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C6: Strukturelle und molekulare Analyse der GlcNac-1-Phosphotransferase

Keywords: mannose 6-phophate; phosphotransferase; sulfotransferase; cytosolic adaptor

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


Prof. Dr. Thomas Braulke / Dr. Stephan Storch

Pavillon 22
Universitätskrankenhaus Eppendorf
20251 Hamburg

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