Pieter Steenhuis
AG Storch
phone: ++49-40-7410 51967 / 52718
email:   Pieter Steenhuis





I study intracellular trafficking of the lysosomal membrane protein CLN7. Mutations in the CLN7 gene cause a form a neuronal ceroid lipofuscinosis, which is a neurodegenerative lysosomal storage disease in children. Several lysosomal targeting sequences were recently identified in the CLN7 protein and I want to determine how these sequences establish correct targeting of CLN7 to the endosomal/lysosomal compartment. I also want to determine the identity of CLN7-positive organelles in neuronal projections, which appear to be different from endosomes and lysosomes.





Judith Koliwer
AG Kreienkamp
phone: ++49-40-7410 57822
email:   Judith Koliwer




In my project, I will analyze the role of PDZ-domain containing proteins in the subcellular sorting of membrane proteins. I will elucidate the interactions that lead to the sorting of membrane proteins to different cell compartments in HEK293, as well as in neuronal cells. My focus will be G-protein coupled receptors, such as β1AR and SSTR5 as well as postsynaptic membrane proteins such as neuroligins or stargazin, all of which have already been shown to interact with one or several PDZ domain proteins.





Sven Flemming
AG Spielmann
phone: ++49-40-42818 490
email:   Sven Flemming





The blood stage of the human malaria parasite /Plasmodium falciparum/ is responsible for the symptoms of the disease. During this stage the parasite resides within red blood cells and feeds on hemoglobin. I am interested in the uptake process of hemoglobin into the food vacuole and would like to elucidate the mechanisms behind this process.





Raffaella de Pace
AG Pohl
phone: +49-40-7410 51968
email:   Raffaella de Pace





The GlcNAc-1-phosphotransferase complex is composed of six subunits, α2β2γ2, playing a key role in the generation of mannose 6-phosphate recognition marker on lysosomal hydrolases. 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 my 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.





Clemens Falker
AG Glatzel
phone: +49-40-7410 54424
email:   Clemens Falker




During prion disease the cellular prion protein (PrPC) is converted to a beta-sheet rich protease resistant form (PrPSc), which leads to severe pathologies in the brain. Both isoforms of the prion protein are transported from cell to cell via exosomes. Using a PrPC knockout model it has been shown that PrPC participates in uptake and intracellular sorting of exosomes in neurons. During my PhD thesis I want to identify PrPC interacting proteins, which are involved in exosomal uptake, sorting and excretion. Further I want to characterize functional domains in PrPC necessary for exosome sorting and trafficking.





Kirstin Albers
AG Heeren
phone: +49-40-7410 59572
email:   Kirstin Albers





The LDL receptor-related protein 1 (LRP1) is implicated in the removal of lipoprotein remnants from plasma. Loss of LRP1 function leads to increased levels of pro-atherogenic plasma lipoproteins. The phosphotyrosine interaction domain-containing protein 1 (PID1) has been identified as an adaptor protein for LRP1, however, the physiological significance of the LRP1-PID1 interaction remains obscure. In my project I would like to investigate the molecular basis of LRP1-PID1 interactions and the consequences of PID1 loss for LRP1 function.





Judith Peters
AG Saftig
phone: +49-431-880-1679
email:   Judith Peters





My project will focus on the lysososomal integral membrane protein type 2 (LIMP-2), which was identified as the receptor for β-glucocerebrosidase that allows the mannose-6-phosphate independent transport of β-glucocerebrosidase from the endoplasmic reticulum to the lysosome. Mutations in LIMP-2 cause the action myoclonus-renal failure syndrome. In my thesis I will focus on the identification and characterization of new interaction partners of LIMP-2 beside β-glucocerebrosidase. In a yeast-2-hybrid screen we already identified several different promising putative interaction partners of LIMP-2, which will be analyzed in future in more detail.





Friederike Zunke
AG Schwake
phone: +49-431-880-2219
email:   Friederike Zunke





My project focuses on the structural and functional analysis of the lysosomal integral membrane protein 2 (LIMP-2). Although LIMP-2 has been shown to be a transporter of β-glucocerebrosidase to the lysosome, binding details are still unknown. A coiled-coil (CC) domain within the luminal site of LIMP-2 has been described as an interaction motif of both proteins. Therefore my work will mainly focus on this part of the protein and interaction studies will include co-crystallisation and transgenic mouse models.





Anja Röder
AG Aepfelbacher
phone: ++49-40-7410 55919
email:   Anja Röder




The function of the Rho GTPase regulator CDC42GAP in phagocytes and endothelial cells is the focus of my project. Preliminary experiments suggest that CDC42GAP is Golgi associated and transported to phagocytic cups as well as to phagosomes in endothelial cells and to unknown vesicular structures in activated human macrophages. The phagosomes we investigate are formed after integrin-triggered phagocytosis of bacterial pathogens (S. aureus, Yersinia). Thus these mechanisms will also play a role in cellular uptake and recycling of integrins.





Kristina Brand
AG Kutsche
phone: +49-40-7410 57822
email:   Kristina Brand




In my project I will focus on the analysis of endocytosis in cells overexpressing various OCRL1 variants, including wild-type and mutants deficient either for the 5-phosphatase activity or in associating with other proteins. I will also use primary fibroblast cells of patients with Lowe syndrome which are OCRL-deficient and study their capacity to internalize numerous ligands, such as transferrin and epidermal growth factor.