C6: Strukturelle und molekulare Analyse der GlcNac-1-Phosphotransferase
The intracellular transport of soluble lysosomal enzymes relies on the post-translational modification of N-linked oligosaccharides to generate mannose 6-phosphate (M6P) residues allowing the binding to M6P-specific receptors. The vesicular transport of receptor-ligand complexes to a prelysosomal compartment is mediated by signal motifs in the cytoplasmic receptor domain interacting with cytoplasmic proteins.
We are interested in
- structural and cell type-specific requirements for an efficient formation of M6P residues catalyzed by the GlcNAc-phosphotransferase
- the identification of structural requirements for the recognition of lysosomal enzymes by the phosphotransferase
- the functional role of a novel 55 kDa cytosolic protein interacting with the M6P receptor
- the role of oligosaccharide sulfation for the transport of lysosomal arylsulfatase A
Contact:
Prof. Dr. Thomas Braulke / Dr. Stephan StorchAddress:
Kinderklinik
Pavillon 22
Universitätskrankenhaus Eppendorf
Martinistr.52
20251 Hamburg
Telefon: 040-42803 4493 (TB)
Telefon: 040-42803 5947 (SS)
Telefax: 040-42803-8504
E-Mail: braulke@uke.uni-hamburg.de; storch@uke.uni-hamburg.de
http://www.uke.uni-hamburg.de/zentren/frauen_kinder_jugendmedizin/kinderklinik/molekularbiologie/index.de.html