Research Training Group 1459

Sorting and Interactions between Proteins of Subcellular Compartments

The Research Training Group 1459 is formed by scientists from the University Medical Center Hamburg-Eppendorf, the Institute of Biochemistry at the niversity Kiel, and the Bernhard-Nocht-Institute for Tropical Medicine in Hamburg. Its program is open to students with a diploma/master in natural sciences and to medical students.

The general topic of the RTG is sorting and transport of selected proteins within the Golgi apparatus and endosomal compartments. In these organelles the decision is made whether a newly synthesized protein reaches its target via the secretory/biosynthetic pathway, or a recently internalized molecule (or bacterium) reaches its intracellular destination via the endocytic/phagocytic pathway. Missorted proteins may lead to loss of function in their target organelles affecting the well being of the cell and the organism as a whole cours de l’argent.

By focussing on selected model proteins, basic mechanisms of the biogenesis of intracellular compartments as well as the balance of membrane transport between organelles and the interplay between cytosolic and membrane proteins are investigated. The majority of projects addresses sorting and transport processes under pathological conditions in cells derived from patients or mouse models of human diseases or cells infected by bacteria or in parasite cells. New insights into the interactions between resident proteins of endosomes and the Golgi apparatus with components of the vesicular transport machinery and the actin cytoskeleton will be expected. A better understanding of cellular responses to endogenous mutant proteins or exogenous pathogens will enable the development of novel therapeutic strategies. Different experimental approaches such as ultrastructural analysis of cellular compartments, genomics, biochemistry, time-resolved imaging, and structural biology will be applied and improve our understanding of spatial and dynamic aspects of membrane transport or translocation. A detailed list of projects and research groups involved is given.

Students will go through a three year curriculum of academic as well as non-academic courses in molecular and cellular biology, biochemistry, infectiology, microbiology, and molecular biomedicine. The Research Training Group offers a continuous educational program with lectures, practical courses, seminars given by leading national and international scientists, regular report meetings and an international symposium every second year. It is expected that each student spends 1-3 months abroad in a laboratory cooperating in the research field. The program provides a broad education, not just on the specific topic of the thesis, but also in research topics of the other participating groups. Active participitation and engagement of the students in the design of this curriculum will strengthen their scientific independence and international competitiveness.

This graduate program started in May 2008 and ended in April 2017.

The scientific program of the Research Training Group 1459 was embedded in research
interests of:

Collaborative Research Center 877
Proteolysis as a Regulatory Event in Pathophysiology


Aepfelbacher group

Spatiotemporal control of bacterial phagocytosis and phagosome maturation
Martin Aepfelbacher, Department of Medical Microbiology, Virology and Hygiene, University Medical Center Hamburg-Eppendorf
webpage Aepfelbacher group

Unique signalling complexes are assembled at the contact site of pathogenic bacteria and host cells and control bacterial invasion and phagosome maturation. We study the dynamic recruitment of a regulator of the Rho GTP-binding protein CDC42, CDC42GAP, to the bacterial uptake site as well as to the bacteria loaded phagosome in endothelial cells. CDC42GAP is bound to recycling endosomes and through the delivery to the phagocytic cup controls local Cdc42 activity. Cdc42 acts back on the delivery of the Cdc42GAP by regulating the exocyst complex that tethers the recycling endosomes to the phagocytic cup. How this regulatory cycle is functioning on the molecular level is in the center of our interest. To study this process a combination of cell biological, biochemical and microbiological techniques is applied.

Glatzel group

Exosomal transports of prions
Markus Glatzel, Institute of Neuropathology, University Medical Center Hamburg-Eppendorf
webpage Glatzel group

Prion diseases are fatal neurodegenerative disorders which are transmissible. An essential part of the infectious agent, termed the prion, is composed of an abnormal isoform of the host-encoded cellular prion-protein termed PrPSc. The molecular details underlying PrPSc formation and the mechanisms involved in the spread of infectious prions within affected hosts and from donor to host are poorly understood. Recently, exosomes have been shown to mobilize PrPSc as well as prion infectivity. Moreover retroviral infection increases exosome formation and virions have been shown to contain PrPSc. The project focus on the investigation of the role of exosomes in secretion of cellular- and disease-associated forms of the prion protein.

Heeren group

Regulation of lipoprotein uptake into liver and brown adipose tissue
Jörg Heeren, Department of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf
webpage Heeren group (in German)

Abnormalities in lipid and lipoprotein metabolism are associated with the development of atherosclerosis and the metabolic syndrome. The uptake and intracellular processing of lipoproteins into liver and brown adipose tissue directly influence plasma lipoprotein levels. These processes are mediated by lipoprotein receptors such as CD36, LDL receptor and the LDL receptor-related protein 1 (LRP1) in dependence on intracellular adaptor proteins. In this project we want to investigate how lipoprotein receptor function and lipid uptake processes are regulated with the focus on endosomal trafficking in hepatocytes and brown adipocytes.

Kneussel group

Role of microtubule turnover in cytoskeleton-mediated sorting and transport of synaptic proteins
Matthias Kneussel, Institute of Molecular Neurogenetics, Center for Molecular Neurobiology Hamburg (ZMNH)
webpage Kneussel group

Fundamental cellular functions, such as motility and division depend on the dynamic behavior of microtubules (MTs). MTs also regulate the sorting and transport of proteins to subcellular compartments inside cells. In neurons, the GluA2 subunit of AMPA receptors (AMPARs) is a key factor of excitatory synaptic transmission. Changes in postsynaptic AMPAR numbers contribute to long-lasting changes in synaptic strength including long-term potentiation (LTP) and long-term depression (LTD). To reach the synapse, GluA2 requires microtubule transport through the kinesin motor protein KIF5. We ask, whether and how the microtubule-severing enzyme spastin participates in the regulation of microtubule transport to synaptic sites. In humans, mutations associated with the spastin gene cause the most frequent form of autosomal dominant spastic paraplegia, an inherited disease whose main feature is progressive stiffness and contraction (spasticity) in the lower limbs, as a result of damage to or dysfunction of the nerves. Using conditional knockout of the AAA ATPase spastin in mice, we aim to investigate whether altered MT turnover affects receptor delivery and consequently synaptic function. Our project combines mouse genetics with live cell imaging and FRAP imaging in neurons. Cell biological studies at the neuron and synapse level are complemented with electrophysiology and the analysis of learning and memory.

Kreienkamp group

Regulated sorting of plasma membrane receptors through the Golgi-associated protein PIST
Hans-Jürgen Kreienkamp, Institute of Human Genetics, University Medical Center Hamburg-Eppendorf
webpage Kreienkamp group (in German)

PIST/GOPC is a Golgi protein which has been implicated in in the sorting and intracellular transport of various receptor proteins. PIST is tethered to the trans-Golgi network through interactions with the GTPase Rab6 and syntaxin-6; in neurons it is present in somatic TGN and in Golgi outposts. Live cell imaging and biochemical assays indicate that PIST is stationary at these sites and does not participate in vesicular transport to the plasma membrane. We will analyze the relevance of PIST for targeting of receptors to postsynaptic sites in neurons. In particular, we will determine how the distribution of PIST-associated membrane proteins neuroligin-2 and stargazin is altered in the absence of PIST, and how PIST contributes to the regulation of membrane protein availibility at the cell surface. These experiments will contribute to our understanding of synapse formation and synaptic plasticity.

Linder group

Rab and motor protein dependent intracellular processing of Borrelia
burgdorferi by primary human macrophages
Stefan Linder, Department of Medical Microbiology, Virology and Hygiene, University Medical Center Hamburg-Eppendorf
webpage Linder group

The spirochete Borrelia burgdorferi is the causative agent of Lyme disease, a multisystemic disorder affecting the skin, nervous system and joints. In this project, we investigate the pathways regulating the intracellular processing of Borreliae by macrophages. In particular, we focus on the role of RabGTPases and microtubule-associated motor proteins of the kinesin and dynein families in the maturation of Borrelia-containing phagolysosomes. It is currently unknown which Rab or kinesin isoforms are involved or essential for the intracellular handling of Borrelia by macrophages. Moreover, from a general cell biological point of view, the intersection of RabGTPase signalling with microtubule-dependent transport of Rab-containing vesicles is largely unexplored. Intracellular handling of the large and easily visible Borrelia phagosomes is thus also a welcome model system to study this field. Within this project, we combine both approaches and place particular emphasis on the trafficking of vesicles containing specific RabGTPase isoforms by specific members of the kinesin motor family.

Pohl group

Subunit interactions of the Golgi-resident GlcNac-1-phosphotransferase
Sandra Pohl, Department of Biochemistry, Children’s Hospital, University Medical Center Hamburg-Eppendorf
webpage Pohl group

Mucolipidoses II and II are inherited lysosomal storage disorders which are caused by defects in the Golgi-localized GlcNAc-1-phosphotransferase complex. This enzyme complex is composed of six subunits, α2β2γ2, playing a key role in the generation of mannose 6-phosphate recognition marker on lysosomal hydrolases which are essential for their efficient transport to lysosomes. The membrane-bound α- and β-subunits of the GlcNAc-1-phosphotransferase are catalytically active whereas the function of the soluble γ-subunit is unclear. The aim of this project is to investigate the interactions of the γ-subunit with α- and/or β-subunits and to define structural requirements for protein binding. The functional significance of these interactions will be analyzed in patient or knock-out cells lacking the γ-subunit. Furthermore, the vesicular transport of the three subunits from the ER to the Golgi-apparatus will be examined.

Schwake/Blanz group

LIMP-2: A fascinating lysosomal membrane protein with multiple functions. Analysis of its role in late endocytotic compartments
Michael Schwake/Judith Blanz/Paul Saftig, Faculty for Chemistry (BC III) at the University of Bielefeld and Institute of Biochemistry at the University of Kiel
webpage Institute of Biochemistry – University of Kiel

The highly glycosylated lysosomal integral membrane protein type-2 (LIMP-2/ SCARB2) is an abundant protein of the lysosomal membrane fulfilling diverse functions. Mutations within SCARB2, the gene encoding LIMP-2 were identified as disease causing for the Action Myoclonus Renal Failure Syndrome (AMRF), a progressive myoclonic epilepsy associated with renal failure (Berkovic et al., 2008, Am J Hum Genet). LIMP-2 has been also identified as the receptor for the uptake of the enterovirus 71 and coxsackievirus A16 which are most frequently associated with hand, foot and mouth disease (Yamayoshi et al., 2009, Nat Medicine).

In 2007, we demonstrated that LIMP-2 is the long sought after receptor for mannose-6-phophate independent trafficking of the acid hydrolase β-gluco­cerebrosidase (GC) to the lysosome and that activity of GC is tightly linked to expression of LIMP-2 (Reczek and Schwake et al., 2007, Cell). GC is required for the intralysosomal breakdown of the sphingolipid glucosylceramide (GluCer). Loss of GC activity leads to intralysosomal accumulation of GluCer and Gaucher disease (GD), the most common lysosomal storage disorder. GD is genetically linked to Parkinson`s disease (PD) and mutations in GBA1, the gene encoding GC represent to date the highest genetic risk factor for developing PD. Recently, in collaboration our group has solved the structure of the LIMP-2 ectodomain highlighting a helical bundle as the GC interaction site (Neculai et al., 2014, Nature). In addition, the LIMP-2 structure revealed the presence of a lipid translocating tunnel suggesting an important role of LIMP-2 in lipid metabolism independent of its function as a GC transporter. Since trafficking of GC requires LIMP-2 and genetic variations within the LIMP-2 locus have been linked to synucleinopthies (Hopfner et al., 2013, Movement Disorder and Bras et al., 2014, Human Molecular Genetics) we examined the role of LIMP-2 in α-syn aggregation by using LIMP-2 knockout mice (Rothaug et al., 2014, PNAS).

In LIMP-2-deficient brains, lysosomal GC activity was strongly reduced which was accompanied by pronounced accumulation of lipids including the GC substrate GluCer. GluCer has been suggested to stabilize soluble oligomeric α-syn species thereby promoting neurotoxic aggregation of α-syn which leads to a blockage of ER-Golgi transport of GC forming a pathogenic loop boosting disease progression (Figure 1) (Mazzulli et al., 2011, Cell). In LIMP-2-deficient brains and in primary cultured neurons, we observed aggregation of α-syn, selective shrinkage of dopaminergic (DA) neurons, apoptotic cell death and glial activation. Heterologous expression of lysosomal targeted LIMP-2 increased lysosomal GC activity and concomitantly enhanced α-syn clearance in various cellular systems. In addition, midbrain sections of sporadic PD patients displayed increased levels of LIMP-2 in surviving DA neurons possibly as a compensatory mechanism to overcome impaired targeting of GC to lysosomes (Rothaug et al., 2014, PNAS). Hence, we suggest that targeting of GC to lysosomes can be modulated via its interaction with LIMP-2 which represents a novel therapeutic target for the treatment of synucleinopathies.

Figure 1. Pathogenic feed-forward loop of glucosyl­cera­mide (GluCer) and α-synuclein. LIMP-2 is responsible for lysosomal trafficking of GC. In absence of LIMP-2 or due to expression of dysfunctional GC as it happens in Gaucher disease, lysosomal activity of GC is reduced resulting in an increased concentration of GluCer with­in lysosomes. GluCer sta­bi­lizes soluble α-synuclein oligo­mers, thus retarding its degra­dation. An accumulation of α-synuclein soluble oligomers may form toxic in­soluble fibrils or block ER-Golgi trafficking of newly synthesized pro­teins such as GC causing an intensi­fying pathogenic loop (adop­ted from Mazzulli et al., 2011).

Our current research focuses i) on the impact of LIMP-2 on GC transport to determine the stoichiometry and the structure of the LIMP-2/GC complex, ii) to unravel the role of LIMP-2 in α-syn metabolism and iii) to elucidate unknown functions of this diverse protein by searching for novel interaction partners of LIMP-2 using biochemical and genetic approaches.

Spielmann group

Decoding the molecular mechanisms of endocytic processes in the human
malaria parasite Plasmodium falciparum
Tobias Spielmann, Section Parasitology, Bernhard Nocht Institute for Tropical Medicine
webpage Spielmann group

The pathology of malaria is caused by the development of Plasmodium parasites in human red blood cells. In this part of the life cycle, the parasite invades red blood cells, wherein it grows and multiplies to produce new invasive stages. After host cell rupture, these stages invade new red blood cells to continue the cycle. During its development in red blood cells the parasite ingests most of the host cell cytoplasm (predominantly hemoglobin) and transports the internalised material to a food vacuole for digestion. This prominent process is essential for the parasite to provide nutrients and to create space for growth. Knowledge about this process so far relied predominantly on electron microscopy and inhibitor studies but the actual uptake of host cell cytosol has never been observed in real time. The aim of this project is to visualise the ingestion of host cell cytosol and to shed light on the underlying molecular mechanisms.

Storch group

Sorting and signal-mediated trafficking of the neuronal ceroid lipofuscinosis-
related CLN7 membrane protein
Stephan Storch, Department of Biochemistry, Children’s Hospital, University Medical Center Hamburg-Eppendorf
webpage Storch group

The variant form of late infantile neuronal ceroid lipofuscinosis caused by mutations in the CLN7 gene belongs to a group of autosomal recessive inherited neurodegenerative disorders of childhood, which are characterized by lysosomal storage and the selective damage and loss of neurons. The CLN7 gene product is a ubiquitously expressed multispanning lysosomal membrane protein of unknown function. In this project we want to investigate the lysosomal targeting of CLN7 and the importance of potential cytosolic sorting signals in CLN7 and their interacting partners for sequential sorting between subcellular compartments. Methods include expression analyses, interaction studies with clathrin adaptor subunits and hemicomplexes and modern imaging techniques.




Prof. Dr. Thomas Braulke
University Medical Center Hamburg-Eppendorf
Dept. Biochemistry, Children’s Hospital
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49 40 7410 54493/51967
fax: +49 40 7410 58504

Vice Chairman

Prof. Dr. Paul Saftig
Institute of Biochemistry
Christian Albrechts University Kiel
Olshausenstr. 40
D-24098 Kiel

phone: +49 431 8802 216
fax: +49 431 8802 238

External Advisory Board

Prof. Dr. Oliver Daumke
Max Delbrück Center for Molecular Medicine
Robert-Rössle-Str. 10
D-13092 Berlin

Prof. Dr. Albert Haas
Institute for Cell Biology
University of Bonn
Ulrich-Haberland-Str. 61a
D- 53121 Bonn

Prof. Dr. Blanche Schwappach
University Medical Center Göttingen
Dept. of Molecular Biology
Humboldtallee 23
D-37073 Göttingen
email:  blanche.schwappach@med.uni-goett



Principle Investigators

Prof. Dr. Martin Aepfelbacher
University Medical Center Hamburg-Eppendorf
Institute of Medical Microbiology, Virology and Hygiene
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49-40-7410 52150
fax: +49-40-7410 54881

Dr. Judith Blanz
Christian Albrechts University Kiel
Institute of Biochemistry
Otto-Hahn-Platz 9
D-24118 Kiel

phone: +49-431-880 2218
fax: +49-431-880 2238

Prof. Dr. Thomas Braulke
University Medical Center Hamburg-Eppendorf
Dept. Biochemistry, Children’s Hospital
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49 40 7410 54493/58780
fax: +49 40 7410 58504

Prof. Dr. Markus Glatzel
University Medical Center Hamburg-Eppendorf
Institute of Neuropathology
Martinistr. 52, Bldg O50
D-20246 Hamburg

phone: +49-40-7410 57583
fax: +49-40-7410 54929

Prof. Dr. Jörg Heeren
University Medical Center Hamburg-Eppendorf
Department of Biochemistry and Molecular Cell Biology
Martinistr. 52
D-20246 Hamburg

phone: +49-40-7410 54745
fax: +49-40-7410 54592

Prof. Dr. Matthias Kneussel
Center for Molecular Neurobiology Hamburg (ZMNH)
Institute of Molecular Neurogenetics
Falkenried 94
D-20251 Hamburg

phone: +49-40-7410 56275
fax: +49-40-7410 57700

Prof. Dr. Hans-Jürgen Kreienkamp
University Medical Center Hamburg-Eppendorf
Institute of Human Genetics
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49-40-7410 55098
fax: +49-40-7410 54395

Prof. Dr. Stefan Linder
University Medical Center Hamburg-Eppendorf
Institute of Medical Microbiology, Virology and Hygiene
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49-40-7410 55175
fax: +49-40-7410 54881

Dr. Sandra Pohl
University Medical Center Hamburg-Eppendorf
Dept. Biochemistry, Children’s Hospital
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49-40-7410 58780
fax: +49-40-7410 58504

Prof. Dr. Paul Saftig
Christian Albrechts University Kiel
Institute of Biochemistry
Olshausenstr. 40
D-24098 Kiel

phone: +49 431 8802 216
fax: +49 431 8802 238

PD Dr. Michael Schwake

present address:
Universität Bielefeld
Fakultät für Chemie, BCIII
Universitätsstr. 25
D-33615 Bielefeld

phone: +49-(0)521-106 2091
fax: +49-(0)521-106 6014

Dr. Tobias Spielmann
Bernhard Nocht Institute for Tropical Medicine
Section Parasitology
Bernhard-Nocht-Str. 74
D-20359 Hamburg

phone: +49-40-42818 486
fax: +49-40-42818 512

PD Dr. Stephan Storch
University Medical Center Hamburg-Eppendorf
Dept. Biochemistry, Children’s Hospital
Martinistr. 52, Bldg. N27
D-20246 Hamburg

phone: +49-40-7410 51967
fax: +49-40-7410 58504


Dr. Dorthe Labonté
University Medical Center Hamburg-Eppendorf
Dept. Biochemistry, Children’s Hospital
Martinistr. 52, Bldg. N27
20246 Hamburg

phone: +49-40-7410 58780
fax: +49-40-7410 58504

Educational Program



Practical courses


Stay abroad


International Symposium
„Protein Trafficking in Health and Disease“
Every second year the RTG1459 hosts the international symposium „Protein Trafficking on Health and Disease“ for approximately 160 PhD students and young Postdocs from all over Europe/the world. The graduate students of the RTG are strongly involved in the organization of the symposium’s 3-day-program – from invitation of speakers and production of an abstract booklet production to fund raising and advertisement design.

In the last years outstanding international scientists presented their data on topics like the Golgi apparatus, vesicular transport, endocytosis, endosomes, lysosomes and infection. Young scientists had the opportunity to present their research projects in selected oral presentations or poster sessions, communicate with each other, discuss technical problems, and find collaboration partners at this international symposium.

The 4th International Symposium took place in Hamburg from June 7th – 9th 2017 and was the final Symposium organized by the RTG1459. Further information can be found on the website

Former Symposia „Protein Trafficking in Health and Disease“

  1. International Symposium 2014

  2. International Symposium 2012

  3. International Symposium 2010

Other Symposia organized by the RTG1459

Lysosomes-meeting 2011


(GRK1459 members marked with *)

[114] Disease-linked lysine glutarylation impairs function and interactions of mitochondrial proteins and contribute to mitochondrial heterogeneity. Schmiesing J, Storch S*, Dörfler AC*, Schweizer M, Makrypidi-Fraune G, Thelen M, Sylvester M, Gieselmann V, Meyer-Schwesinger C, Koch-Nolte F, Tidow H, Mühlhausen C, Waheed A, Sly WS, Braulke T* (2018) Cell Rep in press

[113] Lipolysis Triggers a Systemic Insulin Response Essential for Efficient Energy Replenishment of Activated Brown Adipose Tissue in Mice. Heine M, Fischer AW*, Schlein C, Jung C, Straub LG, Gottschling K, Mangels N*, Yuan Y, Nilsson SK, Liebscher G, Chen O, Schreiber R, Zechner R, Scheja L, Heeren J* (2018) Cell Metab pii: S1550-4131(18)30402-9. Abstract

[112] Rab18 is not necessary for lipid droplet biogenesis or turnover in human mammary carcinoma cells. Jayson CBK, Arlt H, Fischer AW*, Lai ZW, Farese RV, Walther TC (2018) Mol Biol Cell doi: 10.1091/mbc.E18-05-0282 Abstract

[111] The adaptor protein PID1 regulates receptor-dependent endocytosis of postprandial triglyceride-rich lipoproteins. Fischer AW#, Albers K#, Krott LM*, Hoffzimmer B*, Heine M, Schmale H, Scheja L, Gordts PLSM, Heeren J* (2018) Mol Metab doi: 10.1016/j.molmet.2018.07.010. Abstract (#equal contributation)

[110] Lysosomal proteome and secretome analysis identifies missorted enzymes and their non-degraded substrates in mucolipidosis III mouse cells. Di Lorenzo G*, Voltolini Velho R, Winter D, Thelen M, Ahmadi S, Schweizer M, De Pace R*, Cornils K, Yorgan TA, Grüb S, Hermans-Borgmeyer I, Schinke T, Müller-Loennies S, Braulke T*, Pohl S*(2018) Mol Cell Proteomics doi: 10.1074/mcp.RA118.000720. Abstract

[109] Integrin-based diffusion barrier separates membrane domains enabling the formation of microbiostatic frustrated phagosomes. Maxson ME, Naj X*, O’Meara TR, Plumb JD, Cowen LE, Grinstein S (2018) Elife 7: e34798. Abstract

[108] Loss of CLN7 results in depletion of soluble lysosomal proteins and impaired mTOR reactivation. Danyukova T, Ariunbat K*, Thelen M, Brocke-Ahmadinejad N, Mole SE, Storch S* (2018) Hum Mol Genet 27: 1711-22. Abstract

[107] Lrp1 in osteoblasts controls osteoclast activity and protects against osteoporosis by limiting PDGF-RANKL signaling. Bartelt A*, Behler-Janbeck F, Beil FT, Koehne T, Müller B*, Schmidt T, Heine M, Ochs L, Yilmaz T, Dietrich M, Tuckermann JP, Amling M, Herz J, Schinke T, Heeren J*, Niemeier A (2018) Bone Res 6: 4 Abstract

[106] Lysosomal integral membrane protein-2 as a phospholipid receptor revealed by biophysical and cellular studies. Conrad KS, Cheng TW, Ysselstein D, Heybrock S*, Hoth LR, Chrunyk BA, Am Ende CW, Krainc D, Schwake M*, Saftig P*, Liu S, Qiu X, Ehlers MD (2017) Nat Commun 8: 1908 Abstract

[105] Disease-causing mutations affecting surface residues of mitochondrial glutaryl-CoA dehydrogenase impair stability, heteromeric complex formation and mitochondria architecture. Schmiesing J, Lohmöller B*, Schweizer M, Tidow H, Gersting SW, Muntau AC, Braulke T*, Mühlhausen C (2017) Hum Mol Genet 26: 538-51 Abstract

[104] Diverse functions of the prion protein – Does proteolytic processing hold the key? (Review) Linsenmeier L, Altmeppen HC, Wetzel S, Mohammadi B*, Saftig P*, Glatzel M* (2017) Biochim Biophys Acta 1864: 2128-37 Abstract

[103] Functional assays for the assessment of the pathogenicity of variants in GOSR2, an ER-to-Golgi SNARE involved in progressive myoclonus epilepsies. Völker JM*, Dergai M, Abriata LA, Mingard Y, Ysselstein D, Krainc D, Dal Peraro M, von Mollard GF, Fasshauer D, Koliwer J*, Schwake M* (2017) Dis Model Mech pii: dmm.029132. doi: 10.1242/dmm.029132. Abstract

[102] Site-1 protease and lysosomal homeostasis. (Review) Velho RV, De Pace R*, Klünder S*, Di Lorenzo G*, Schweizer M, Braulke T*, Pohl S* (2017) Biochim Biophys Acta pii: S0167-4889(17)30186-6 Abstract

[101] SHANK proteins limit integrin activation by directly interacting with Rap1 and R-Ras. Lilja J, Zacharchenko T, Georgiadou M, Jacquemet G, Franceschi N, Peuhu E, Hamidi H, Pouwels J, Martens V*, Nia FH, Beifuss M*, Boeckers T, Kreienkamp HJ*, Barsukov IL, Ivaska J (2017) Nat Cell Biol 19:292-305 Abstract

[100] A genetic system to study Plasmodium falciparum protein function. Birnbaum J, Flemming S*, Reichard N, Soares AB*, Mesén-Ramírez P, Jonscher E*, Bergmann B, Spielmann T* (2017) Nat Methods 14:450-6 Abstract

[99] Substrate-analogous inhibitors exert antimalarial action by targeting the Plasmodium lactate transporter PfFNT at nanomolar scale. Golldack A, Henke B, Bergmann B, Wiechert M, Erler H, Blancke Soares A*, Spielmann T*, Beitz E (2017) PLoS Pathog 13:e1006172 Abstract

[98] Progress in imaging methods: insights gained into Plasmodium biology. (Review) De Niz M, Burda PC, Kaiser G, Del Portillo HA, Spielmann T*, Frischknecht F, Heussler VT (2017) Nat Rev Microbiol 15:37-54 Abstract

[97] Acting on Actin: Rac and Rho Played by Yersinia. (Review) Aepfelbacher M*, Wolters M (2017) Curr Top Microbiol Immunol 399:201-220 Abstract

[96] Disruption of the v-H±ATPase complex in liver causes MTORC1-independent accumulation of autophagic vacuoles and lysosomes. Kissing S*, Rudnik S*, Damme M, Lüllmann-Rauch R, Ichihara A, Kornak U, Eskelinen EL, Jabs S, Heeren J*, De Brabander J, Haas A, Saftig P* (2017) Autophagy 13:670-85 Abstract

[95] Quantitative proteome analysis of mouse liver lysosomes provides evidence for mannose 6-phosphate-independent targeting mechanisms of acid hydrolases in mucolipidosis II. Markmann S#, Krambeck S#, Hughes CJ, Mirzaian M, Aerts JM, Saftig P*, Schweizer M, Vissers JC, Braulke T*, Damme M (2017) Mol Cell Proteomics 16:438-450 Abstract (#equal contributation)

[94] Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase. Velho RV, De Pace R*, Tidow H, Braulke T*, Pohl S* (2016) FEBS Lett 23: 4287-95 Abstract

[93] Parkinson’s disease: acid-glucocerebrosidase activity and alpha-synuclein clearance. (Review) Blanz J*, Saftig P* (2016) J Neurochem 139 Suppl 1: 198-215. Abstract

[92] Branch-Specific Microtubule Destabilization Mediates Axon Branch Loss during Neuromuscular Synapse Elimination. Brill MS#, Kleele T#, Ruschkies L*#, Wang M, Marahori NA, Reuter MS, Hausrat TJ, Weigand E, Fisher M, Ahles A, Engelhardt S, Bishop DL, Kneussel M*, Misgeld T (2016) Neuron 92:845-56 Abstract (#joint first authors)

[91] Endocannabinoid regulation in white and brown adipose tissue following thermogenic activation. Krott LM*, Piscitelli F, Heine M, Borrino S, Scheja L, Silvestri C, Heeren J*, Di Marzo V (2016) J Lipid Res 57: 464-73 Abstract

[90] Retinal Degeneration in Mice Deficient in the Lysosomal Membrane Protein CLN7. Jankowiak W, Brandenstein L*, Dulz S, Hagel C, Storch S*, Bartsch U (2016) Invest Ophthalmol Vis Sci 57: 4989-98 Abstract

[89] Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. Rauch L*, Hennings K, Trasak C, Röder A*, Schröder B, Koch-Nolte F, Rivera-Molina F, Toomre D, Aepfelbacher M* (2016) J Cell Sci 129: 2937-49 Abstract

[88] Immunosuppressive Yersinia Effector YopM Binds DEAD Box Helicase DDX3 to Control Ribosomal S6 Kinase in the Nucleus of Host Cells. Berneking L*, Schnapp M, Rumm A, Trasak C, Ruckdeschel K, Alawi M, Grundhoff A, Kikhney AG, Koch-Nolte F, Buck F, Perbandt M, Betzel C, Svergun DI, Hentschke M, Aepfelbacher M* (2016) PLoS Pathog 12: e1005660 Abstract

[87] Actin regulation during phagocytosis of Borrelia burgdorferi by macrophages. Naj X*, Linder S* (2016) Curr Top Microbiol Immunol Abstract

[86] The machinery underlying malaria parasite virulence is conserved between rodent and human malaria parasites. De Niz M, Ullrich AK, Heiber A, Blancke Soares A*, Pick C, Lyck R, Keller D, Kaiser G, Prado M, Flemming S*, Del Portillo H, Janse CJ, Heussler V, Spielmann T* (2016) Nat Commun 7: 11659 Abstract

[85] Stable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation Activity. Mesén-Ramírez P, Reinsch F*, Blancke Soares A*, Bergmann B, Ullrich AK, Tenzer S, Spielmann T* (2016) PLoS Pathog 12: e1005618 Abstract

[84] Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding. Boddey JA, O’Neill MT, Lopaticki S, Carvalho TG, Hodder AN, Nebl T, Wawra S, van West P, Ebrahimzadeh Z, Richard D, Flemming S*, Spielmann T*, Przyborski J, Babon JJ, Cowman AF (2016) Nat Commun 7: 10470 Abstract

[83] Characterization of the complex formed by β-glucocerebrosidase and the lysosomal integral membrane protein type-2. Zunke F*, Andresen L, Wesseler S*, Groth J*, Arnold P, Rothaug M*, Mazzullic JR, Krainc D, Blanz J*, Saftig P*, Schwake M* (2016) Proc Natl Acad Sci U S A doi:10.1073/pnas.1514005113 Abstract

[82] Lysosomal dysfunction and impaired autophagy in a novel mouse model deficient for the lysosomal membrane protein Cln7. Brandenstein L*, Schweizer M, Sedlacik J, Fiehler J, Storch S* (2016) Hum Mol Genet 25: 777-91 Abstract

[81] Hierarchical phosphorylation of apical membrane antigen 1 is required for efficient red blood cell invasion by malaria parasites. Prinz B, Harvey KL, Wilcke L, Ruch U*, Engelberg K, Biller L, Lucet I, Erkelenz S, Heincke D, Spielmann T*, Doerig C, Kunick C, Crabb BS, Gilson PR, Gilberger TW* (2016) Sci Rep 6: 34479 Abstract

[80] Exosomal PrP© drives fibrillization of amyloid beta and counteracts amyloid beta-mediated neurotoxicity. Falker C*, Hartmann A, Guett I*, Dohler F, Altmeppen H, Betzel C, Schubert R, Thurm D*, Wegwitz F, Joshi P, Verderio C, Krasemann S, Glatzel M* (2016) J Neurochem 137: 88-100 Abstract

[79] αPIX Is a Trafficking Regulator that Balances Recycling and Degradation of the Epidermal Growth Factor Receptor. Kortüm F*, Harms FL, Hennighausen N, Rosenberger G (2015) PLoS One 10: e0132737 Abstract

[78] Vacuolar ATPase in phagosome-lysosome fusion. Kissing S*, Hermsen C, Repnik U, Nesset CK, von Bargen K, Griffiths G, Ichihara A, Lee BS, Schwake M*, De Brabander J, Haas A, Saftig P* (2015) J Biol Chem 290: 14166-80. Abstract

[77] Critical Steps in Protein Export of Plasmodium falciparum Blood Stages. (Review) Spielmann T*, Gilberger TW* (2015) Trends Parasitol 31: 514-25. Abstract

[76] Chronic enzyme replacement therapy ameliorates neuropathology in alpha-mannosidosis mice. Damme M, Stroobants S, Lüdemann M, Rothaug M*, Lüllmann-Rauch R, Beck HC, Ericsson A, Andersson C, Fogh J, D’Hooge R, Saftig P*, Blanz J* (2015) Ann Clin Transl Neurol 2: 987-1001. Abstract

[75] LAMP-2 deficiency leads to hippocampal dysfunction but normal clearance of neuronal substrates of chaperone-mediated autophagy in a mouse model for Danon disease. Rothaug M*, Stroobants S, Schweizer M, Peters J*, Zunke F*, Allerding M, D’Hooge R, Saftig P*, Blanz J* (2015) Acta Neuropathol Commun 3: 6 Abstract

[74] Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Peters J*, Rittger A, Weisner R, Knabbe J*, Zunke F*, Rothaug M*, Damme M, Berkovic SF, Blanz J*, Saftig P*, Schwake M* (2015) Biochem Biophys Res Commun 457: 334-40 Abstract

[73] Subunit interactions of the disease-related hexameric GlcNAc-1-phosphotransferase complex. De Pace R*, Velho RV, Encarnação M*, Marschner K*, Braulke T*, Pohl S* (2015) Hum Mol Genet 24: 6826-35 Abstract

[72] Shedding light on prion disease. (Review) Glatzel M*, Linsenmeier L, Dohler F, Krasemann S, Puig B, Altmeppen HC (2015) Prion 9: 244–56 Abstract

[71] ER-Coordinated Activities of Rab22a and Rab5a Drive Phagosomal Compaction and Intracellular Processing of Borrelia burgdorferi by Macrophages. Naj X*, Linder S* (2015) Cell Rep 12: 1-15 Abstract

[70] Mannose 6-phosphate-independent lysosomal sorting of LIMP-2. Blanz J*, Zunke F*, Markmann S*, Damme M, Braulke T*, Saftig P*, Schwake M* (2015) Traffic 16: 1127-36 Abstract

[69] Site-1 protease-activated formation of lysosomal targeting motifs is independent of the lipogenic transcription control. Klünder S*, Heeren J*, Markmann S*, Santer R, Braulke T*, Pohl S* (2015) J Lipid Res 56: 1625-32 Abstract

[68] Identity of a Plasmodium lactate/Hþ symporter structurally unrelated to human transporters. Wu B, Rambow J, Bock S, Holm-Bertelsen J, Wiechert M, Blancke Soares A*, Spielmann T*, Beitz E (2015) Nat Comm 6: 6284 Abstract

[67] Genetic Dissection of Tissue-Specific Apolipoprotein E Function for Hypercholesterolemia and Diet-Induced Obesity. Wagner T, Bartelt A*, Schlein C*, Heeren J* (2015) PLoS One 10: e0145102 Abstract

[66] Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site. Velho RV, De Pace R*, Klünder S*, Sperb-Ludwig F, Lourenço CM, Schwartz IV, Braulke T*, Pohl S* (2015) Hum Mol Genet 24: 3497-505 Abstract

[65] Apolipoprotein E promotes lipid accumulation and differentiation in human adipocytes. Lasrich D*, Bartelt A*, Grewal T, Heeren J* (2015) Exp Cell Res 337: 94-102 Abstract

[64] Lrp1/LDL receptor play critical roles in mannose 6-phosphate-independent lysosomal enzyme targeting. Markmann S*, Thelen M, Cornils K, Schweizer M, Brocke-Ahmadinejad N, Willnow T, Heeren J*, Gieselmann V, Braulke T*, Kollmann K (2015) Traffic 16: 743-59 Abstract

[63] The Golgi-associated PDZ domain protein PIST/GOPC stabilizes the
β1-adrenergic receptor in intracellular compartments after internalization.
Koliwer J*, Park M, Bauch C*, von Zastrow M, Kreienkamp HJ* (2015) J Biol Chem 290: 6120-9 Abstract

[62] Biosynthesis, targeting, and processing of lysosomal proteins: Pulse-chase labeling and immune precipitation. Pohl S*, Hasilik A (2015) Methods Cell Biol 126: 63-83 Abstract

[61] Autophagy in neuronal cells: general principles and physiological and pathological functions. (Review) Damme M, Suntio T, Saftig P*, Eskelinen EL (2014) Acta Neuropathol 129: 337-62 Abstract

[60] LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance. Rothaug M*, Zunke F*, Mazzulli JR, Schweizer M, Altmeppen H, Lüllmann, Rauch R, Kallemeijn WW, Gaspar P, Aerts JM, Glatzel M*, Saftig P*, Krainc D, Schwake M*, Blanz J* (2014) Proc Natl Acad Sci U S A 111: 15573-8 Abstract

[59] The GPI-anchoring of PrP: implications in sorting and pathogenesis. (Review) Puig B, Altmeppen H, Glatzel M* (2014) Prion 8: 11-8 Abstract

[58] Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins. Bauch C*, Koliwer J*, Buck F, Hönck HH, Kreienkamp HJ* (2014) PLoS One 9: e88529 Abstract

[57] A role for exocyst in maturation and bactericidal function of staphylococci-containing endothelial cell phagosomes. Rauch L*, Hennings K, Aepfelbacher M* (2014) Traffic 15: 1083-98 Abstract

[56] Daam1 is a regulator of filopodia formation and phagocytic uptake of Borrelia burgdorferi by primary human macrophages. Hoffmann AK, Naj X*, Linder S* (2014) FASEB J 28: 3075-89 Abstract

[55] GRIP1 interlinks N-cadherin and AMPA receptors at vesicles to promote combined cargo transport into dendrites. Heisler FF, Lee HK, Gromova KV, Pechmann Y, Schurek B, Ruschkies L*, Schroeder M, Schweizer M, Kneussel M* (2014) Proc Natl Acad Sci U S A 111: 5030-5 Abstract

[54] Homozygosity for a partial deletion of apoprotein A-V signal peptide results in intracellular missorting of the protein and chylomicronemia in a breast-fed infant.
Albers K*, Schlein C*, Wenner K, Lohse P, Bartelt A*, Heeren J*, Santer R, Merkel M (2014) Atherosclerosis 233: 97-103 Abstract

[53] The lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies. Schipanski A*#, Oberhauser F*#, Neumann M, Lange S, Szalay B, Krasemann S, van Leeuwen FW, Galliciotti G, Glatzel M* (2014) Neurobiol Aging 35: 2394-403 Abstract (#joint first authors)

[52] Mucolipidosis II-Related Mutations Inhibit the Exit from the Endoplasmic Reticulum and Proteolytic Cleavage of GlcNAc-1-Phosphotransferase Precursor Protein (GNPTAB). De Pace R*, Coutinho MF, Koch-Nolte F, Haag F, Prata MJ, Alves S, Braulke T*, Pohl S* (2014) Hum Mutat 35: 368-76 Abstract

[51] Gene disruption of Mfsd8 in mice provides the first animal model for CLN7 disease. Damme M, Brandenstein L*, Fehr S, Jankowiak W, Bartsch U, Schweizer M, Hermans- Borgmeyer I, Storch S* (2014) Neurobiol Dis 65C: 12-24 Abstract

[50] The Legionella effector RidL inhibits retrograde trafficking to promote intracellular replication. Finsel I, Ragaz C, Hoffmann C, Harrison CF, Weber S, van Rahden VA*, Johannes L, Hilbi H (2013) Cell Host Microbe 14: 38-50. Abstract

[49] The tetraspanin CD63 is required for efficient IgE-mediated mast cell degranulation and anaphylaxis. Kraft S, Jouvin MH, Kulkarni N, Kissing S*, Morgan ES, Dvorak AM, Schröder B, Saftig P*, Kinet JP (2013) J Immunol 191: 2871-8. Abstract

[48] Parallel regulation of renin and lysosomal integral membrane protein 2 in renin-producing cells: further evidence for a lysosomal nature of renin secretory vesicles. Schmid J, Oelbe M*, Saftig P*, Schwake M*, Schweda F (2013) Pflugers Arch 465: 895-905. Abstract

[47] Amyloid-precursor-protein-lowering small molecules for disease modifying therapy of Alzheimer’s disease. Rosenkranz SC*, Geissen M, Härter K*, Szalay B, Ferrer I, Vogel J*, Smith S, Glatzel M* (2013) PLoS One 8: e82255. Abstract

[46] A novel interaction between aging and ER overload in a protein conformational dementia. Schipanski A*, Lange S, Segref A, Gutschmidt A, Lomas DA, Miranda E, Schweizer M, Hoppe T, Glatzel M* (2013) Genetics 193: 865-76. Abstract

[45] Myosin motors at neuronal synapses: drivers of membrane transport and actin dynamics (Review). Kneussel M*, Wagner W (2013) Nat Rev Neurosci 14: 233-47 Abstract

[44] Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export. Heiber A, Kruse F, Pick C, Grüring C, Flemming S*, Oberli A, Schoeler H, Retzlaff S, Mesén-Ramírez P, Hiss JA, Kadekoppala M, Hecht L, Holder AA, Gilberger TW*, Spielmann T* (2013) PLoS Pathog 9: e1003546 Abstract

[43] Protein export in malaria parasites: many membranes to cross. (Review) Marti M, Spielmann T* (2013) Curr Opin Microbiol 16: 445-51 Abstract

[42] Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Neculai D, Schwake M*, Ravichandran M, Zunke F*, Collins RF, Peters J*, Neculai M, Plumb J, Loppnau P, Pizarro JC, Seitova A, Trimble WS, Saftig P*, Grinstein S, Dhe-Paganon S (2013) Nature 504: 172-6 Abstract

[41] Lysosomal membrane proteins and their central role in physiology. (Review) Schwake M*, Schröder B, Saftig P* (2013) Traffic 14:739-48 Abstract

[40] Decreased bone formation and increased osteoclastogenesis cause bone loss in mucolipidosis II. Kollmann K, Pestka JM, Kühn SC, Schöne E*, Schweizer M, Karkmann K*, Otomo T, Catala-Lehnen P, Failla AV, Marshall RP, Krause M, Santer R, Amling M, Braulke T*, Schinke T (2013) EMBO Mol Med 5: 1871-86 Abstract

[39] Ultrastructural analysis of neuronal and non-neuronal lysosomal storage in mucolipidosis type II knock-in mice. Schweizer M, Markmann S*, Braulke T*, Kollmann K Ultrastruct Pathol (2013) 37: 366-72 Abstract

[38] Plasmodium falciparum Atg8 implicated in both autophagy and apicoplast formation. Tomlins A, Ben-Rached F, Williams R, Proto W, Coppens I, Ruch U*, Gilberger TW*, Coombs G, Mottram J, Müller M, Gordon Langsley G (2013) Autophagy 9: 1540-52 Abstract

[37] Transport of the GlcNAc-1-phosphotransferase α/β-subunit precursor protein to the Golgi apparatus requires a combinatorial sorting motif. Franke M*, Braulke T*, Storch S* (2013) J Biol Chem 288: 1238-49 Abstract

[36] Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration. Altmeppen HC, Prox J, Puig B, Dohler F, Falker C*, Krasemann S, Glatzel M* (2013) FEBS J 280: 4338-47 Abstract

[35] Uncovering common principles in protein export of malaria parasites. Grüring C, Heiber A, Kruse F, Flemming S*, Franci G, Colombo SF, Fasana E, Schoeler H, Borgese N, Stunnenberg HG, Przyborski JM, Gilberger TW*, Spielmann T* (2012) Cell Host Microbe 12: 717-29 Abstract

[34] Lysosomal dysfunction causes neurodegeneration in mucolipidosis II ‚knock-in‘ mice. Kollmann K, Damme M, Markmann S*, Morelle W, Schweizer M, Hermans-Borgmeyer I, Röchert AK*, Pohl S*, Lübke T, Michalski JC, Käkelä R, Walkley SU, Braulke T* (2012) Brain 135: 2661-75 Abstract

[33] The 5-phosphatase OCRL mediates retrograde transport of the mannose 6-phosphate receptor by regulating a Rac1-cofilin signalling module. van Rahden VA*, Brand K*, Najm J, Heeren J*, Pfeffer SR, Braulke T*, Kutsche K* (2012) Hum Mol Genet 21: 5019-38 Abstract

[32] Impaired LDL receptor-related protein 1 translocation correlates with improved dyslipidemia and atherosclerosis in apoE-deficient mice. Gordts PL, Bartelt A*, Nilsson SK, Annaert W, Christoffersen C, Nielsen LB, Heeren J*, Roebroek AJ (2012) PLoS One 7: e38330 Abstract

[31] Proteolytic processing of the prion protein in health and disease (Review). Altmeppen HC, Puig B, Dohler F, Thurm DK*, Falker C*, Krasemann S, Glatzel M* (2012) Am J Neurodegener Dis 1: 15-31 Abstract

[30] Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7 Steenhuis P*, Froemming J, Reinheckel T, Storch S* (2012) Biochim Biophys Acta 1822: 1617-28 Abstract

[29] Evolution and architecture of the inner membrane complex in asexual and sexual stages of the malaria parasite. Kono M, Herrmann S, Loughran NB, Cabrera A, Engelberg K, Lehmann C, Sinha D, Prinz B, Ruch U*, Heussler V, Spielmann T*, Parkinson J, Gilberger TW* (2012) Mol Biol Evol 29: 2113-32 Abstract

[28] A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase. Zachos C*, Blanz J*, Saftig P*, Schwake M* (2012) Traffic 13: 1113-23 Abstract

[27] A new, powerful player in lipoprotein metabolism: brown adipose tissue (Review). Bartelt A*, Merkel M, Heeren J* (2012) J Mol Med 90: 887-93 Abstract

[26] Low density lipoprotein receptor-related protein 1 dependent endosomal trapping and recycling of apolipoprotein E. Laatsch A, Panteli M, Sornsakrin M, Hoffzimmer B*, Grewal T, Heeren J* (2012) PLoS ONE 7: e29385 Abstract

[25] Regional and subcellular distribution of the receptor-targeting protein PIST/GOPC in the rat central nervous system. Chen A#, Gössling E#, Witkowski L, Bhindi A, Bauch C, Roussy G, Sarret P, Kreienkamp HJ*, Stroh T (2012) J Comp Neurol 520: 889-913 #contributed equally Abstract

[24] The role of apolipoprotein E in bone metabolism (Review). Niemeier A, Schinke T, Heeren J*, Amling M (2012) Bone 50: 518-24 Abstract

[23] A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism. Marschner K*, Kollmann K, Schweizer M, Braulke T*, Pohl S* (2011) Science 333: 87-90 Abstract

[22] Brown adipose tissue activity controls triglyceride clearance. Bartelt A*, Bruns OT, Reimer R, Hohenberg H, Ittrich H, Peldschus K, Kaul MG, Tromsdorf UI, Weller H, Waurisch C, Eychmüller A, Gordts PL, Rinninger F, Bruegelmann K, Freund B, Nielsen P, Merkel M, Heeren J* (2011) Nat Med 17: 200-5 Abstract

[21] Posttranslational modifications of the gamma-subunit affect intracellular trafficking and complex assembly of the GlcNAc-1-phosphotransferase. Encarnação M*, Kollmann K, Trusch M, Braulke T*, Pohl S* (2011) J Biol Chem 286: 5311-18 Abstract

[20] Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo. Altmeppen HC, Prox J, Puig B, Kluth MA, Bernreuther C, Thurm D*, Jorissen E, Petrowitz B, Bartsch U, De Strooper B, Saftig P*, Glatzel M* (2011) Mol Neurodegener 6: 36 Abstract

[19] Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase. Kokkola T, Kruse C, Roy-Pogodzik EM, Pekkinen J, Bauch C*, Hönck HH, Hennemann H, Kreienkamp HJ* (2011) FEBS Lett 585: 2665-70 Abstract

[18] Two dileucine motifs mediate late endosomal/lysosomal targeting of transmembrane protein 192 (TMEM192) and a C-terminal cysteine residue is responsible for disulfide bond formation in TMEM192 homodimers. Behnke J, Eskelinen EL, Saftig P*, Schröder B (2011) Biochem J 434: 219-31 Abstract

[17] The core FOXG1 syndrome phenotype consists of postnatal microcephaly, severe mental retardation, absent language, dyskinesia, and corpus callosum hypogenesis. Kortüm F*, Das S, Flindt M, Morris-Rosendahl DJ, Stefanova I, Goldstein A, Horn D, Klopocki E, Kluger G, Martin P, Rauch A, Roumer A, Saitta S, Walsh LE, Wieczorek D, Uyanik G, Kutsche K*, Dobyns WB (2011) J Med Genet 48: 396-406 Abstract

[16] Altered endocannabinoid signalling after a high-fat diet in Apoe (-/-) mice: relevance to adipose tissue inflammation, hepatic steatosis and insulin resistance. Bartelt A*, Orlando P, Mele C, Ligresti A, Toedter K, Scheja L, Heeren J*, Di Marzo V (2011) Diabetologia 54: 2900-10 Abstract

[15] N-glycans and Glycosylphosphatidylinositol-Anchor Act on Polarized Sorting of Mouse PrPC in Madin-Darby Canine Kidney Cells. Puig B, Altmeppen HC, Thurm D*, Geissen M, Conrad C, Braulke T*, Glatzel M* (2011). PLoS ONE 6: e24624 Abstract

[14] Apolipoprotein A-V; a potent triglyceride reducer. (Review) Nilsson SK, Heeren J*, Olivecrona G, Merkel M (2011) Atherosclerosis 219: 15-21 Abstract

[13] Loss of N-acetylglucosamine-1-phosphotransferase gamma subunit due to intronic mutation in GNPTG causes mucolipidosis type III gamma: Implications for molecular and cellular diagnostics. Pohl S*, Encarnacão M*, Castrichini M, Müller-Loennies S, Muschol N, Braulke T* (2010) Am J Med Genet A 152A: 124-32 Abstract

[12] Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif. Steenhuis P*, Herder S, Gelis S, Braulke T*, Storch S* (2010) Traffic 11: 987-1000 Abstract

[11] Mannose 6-phosphorylation in health and disease (Review). Kollmann K, Pohl S*, Marschner K*, Encarnação M*, Sakwa I, Tiede S, Poorthuis BJ, Lübke T, Müller-Loennies S, Storch S*, Braulke T* (2010) Eur J Cell Biol 89: 117-23 Abstract

[10] Proteolytic processing of the gamma-subunit is associated with the failure to form GlcNAc-1-phosphotransferase complexes and mannose 6-phosphate residues on lysosomal enzymes in human macrophages. Pohl S*, Tiede S, Marschner K*, Encarnação M*, Castrichini M, Kollmann K, Muschol N, Ullrich K, Müller-Loennies S, Braulke T* (2010) J Biol Chem 285: 23936-44 Abstract

[09] Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase. Blanz J*, Groth J*, Zachos C*, Wehling C, Saftig P*, Schwake M* (2010) Hum Mol Genet 19: 563-72 Abstract

[08] Apolipoprotein E-dependent inverse regulation of vertebral bone and adipose tissue mass in C57Bl/6 mice: modulation by diet-induced obesity. Bartelt A*, Beil FT, Schinke T, Roeser K, Ruether W, Heeren J*, Niemeier A (2010) Bone 47: 736-45 Abstract

[07] The proteome of lysosomes (Review). Schröder BA, Wrocklage C, Hasilik A, Saftig P* (2010) Proteomics 10: 4053-76 Abstract

[06] Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways? (Review) Spielmann T*, Gilberger TW*(2010) Trends Parasitol 26: 6-10 Abstract

[05] Sorting of lysosomal proteins (Review). Braulke T*, Bonifacino JS (2009) Biochim Biophys Acta 1793: 605-14 Abstract

[04] Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function (Review). Saftig P*, Klumperman J (2009) Nat Rev Mol Cell Biol 10: 623-35 Abstract

[03] Yersinia enterocolitica differentially modulates RhoG activity in host cells. Roppenser B, Röder A*, Hentschke M, Ruckdeschel K, Aepfelbacher M* (2009) J Cell Sci 122: 696-705 Abstract

[02] Sequence requirements for the export of the Plasmodium falciparum Maurer’s clefts protein REX2. Haase S, Herrmann S, Grüring C, Heiber A, Jansen PW, Langer C, Treeck M, Cabrera A, Bruns C, Struck NS, Kono M, Engelberg K, Ruch U*, Stunnenberg HG, Gilberger TW*, Spielmann T* (2009) Mol Microbiol 71: 1003-17 Abstract

[01] Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases (Review). Pohl S*, Marschner K*, Storch S*, Braulke T*(2009) Biol Chem 390: 521-27 Abstract


Giorgia Di Lorenzo

Young Scientist Award – Oral Presentation, 21st Meeting of the European Study Group on Lysosomal Disorder (ESGLD), Lyon – France
Adriana Gonzalez

Poster Award, 4th International Symposium on „Protein Trafficking in Health and Disease“, Hamburg
Ernst Jonscher

Awarded Oral Presentation, 2nd International Conference on Intracellular Niches of Pathogens, Glashütten
Adriana Gonzalez

Awarded Student Talk, 13th Horizons in Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen
Johannes Knabbe

Dissertationprize of the University of Kiel (Fakultätspreis)
Judith Koliwer

Dissertation Prize Gebhard Koch Preis für Zellbiochemie und Neurobiologie
Xenia Naj

Research Award of the German Borreliosis Society
UKE Paper of the Month September 2015 Abstract
Kirstin Albers

Joachim Ziegenhorn Young Investigator Award (Best Oral Presentation), 37th European Lipoprotein Club, Tutzing
Laura Brandenstein

Poster Award, 14th NCL (Neuronal Ceroid Lipofuscinosis) Conference, Cordoba – Argentina
Raffaella De Pace

Young Scientist’s Award, Meeting of the Working Group for Paediatric Metabolic
Disturbances (APS), Fulda
Kirstin Albers

Joachim Ziegenhorn Young Investigator Award (Poster Award), 36th European Lipoprotein Club, Tutzing
Young Investigator Award for Best Oral Presentation, 19th Annual Scandinavian Atherosclerosis Conference, Humlebaek – Denmark
Sandra Markmann

Young Investigator Award, Meeting of the European Study Group on Lysosomal
Disorder (ESGLD), Graz – Austria
Alexander Bartelt

Young Investigator Award, 80th European Atherosclerosis Society (EAS) Congress,
Milan – Italy
Kathrin Karkmann

Ursula Wachtel Prize, Conference of the Working Group for Paediatric Metabolic
Disorders, Fulda
Sandra Markmann

NIKON Award for the Best Microscopic Image
UKE Paper of the Month September 2012
Vanessa A. van Rahden

UKE Paper of the Month August 2012
Alexander Bartelt

Joachim Ziegenhorn Young Investigator Award, 34th European Lipoprotein Club, Tutzing
Karl Lohmann Prize, Society for Biochemistry and Molecular Biology (GBM)
President´s Poster Competition Award Annual Meeting of the American Society for Bone and Mineral Research (ASBMR), San Diego/CA – USA
Werner Otto Prize for the Advancement of Medical Research
Karl-Heinz Hölzer Prize for Interdisciplinary Medical Research
UKE Paper of the Month January 2011
Elisabeth Schöne

Ursula Wachtel Prize, Conference of the Working Group for Paediatric Metabolic
Disorders, Fulda
Katrin Marschner

Young Investigator Award, Meeting of the European Study Group on Lysosomal
Disorders (ESGLD), Helsinki – Finnland
Hans-Dietrich Herrmann Prize for Molecular Medicine
UKE Paper of the Month July 2011
Alexander Bartelt

New Investigator Award, 9th Conference of the International Society for the Study of
Fatty Acids and Lipids (ISSFAL), Maastricht – Netherlands
New Investigator Award, European Lipoprotein Club, Tutzing
Miriam Wagner

Oral Presentation Award, 1st International Symposium on Protein Trafficking in Health and Disease, Hamburg
Alexander Bartelt

Young Investigator Award, XV. International Symposium on Atherosclerosis,
International Atherosclerosis Society (IAS), Boston/MA – USA
Awards of PIs
Sandra Pohl

Werner Otto Prize for the Advancement of Medical Research
Paul Saftig

Hans & Ilse Breuer Prize for Alzheimer Research

End of Funding

The programme of the Research Training Group 1459 ended on April 30th 2017 after having completed the full funding period of 9 years.