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Fachgebiete: Biologie
Thema: Doktorarbeit: The role of O- and N-linked glycans in the sorting for exosomal export of MUC1
Ansprechpartner: Prof. Franz-Georg Hanisch
Antwort an: franz.hanisch@uni-koeln.de
Institution: Institut für Biochemie
Ort: 50931 Köln, Joseph-Stelzmann-Str. 52

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Cell surface integral membrane glycoproteins, like MUC1, can recycle through the Golgi/TGN to undergo processing of their O- and N-glycosylation profiles or can be exported via multivesicular bodies and exosome release. Both processes can be active in parallel and might be involved in the homeostatic regulation of plasma membranous glycoprotein receptors and their glycosylation. According to our preliminary data, the sorting for either recycling to the plasma membrane or exosomal export correlates with differential processing of the single N-glycan on the small MUC1 subunit. In the current proposal we would like to address the question of whether (a) the distinct N-glycosylation of the small MUC1 subunit and/or (b) O-glycosylation of the MUC1 tandem repeat domain in the large subunit that changes during recycling, are functionally involved in the sorting and targeting of MUC1 for exosomal export. The workplan comprises (1) the mass spectrometric profiling of structural chang
es in N- and O-glycosylation associated with exosomal export of MUC1, the investigation of effects on plasma membranous vs. exosomal expression of MUC1, using deletion mutants lacking the tandem repeat domain (2), lacking an N-glycosylation consensus sequence in the small subunit (3) or (4) using inhibitors of high-mannose N-glycan trimming. (5) Further evidence for a glycosylation-associated MUC1 targeting will be corroborated in live cell imaging studies using GFP-MUC1-transfected cell models with modulated N-/O-glycosylation.

Methoden:
mutant MUC1 construct generation and recombinant expression in HEK293 and breast cancer cell lines,
cell surface biotinylation & western blotting confocal microscopy, life cell imaging

Anfangsdatum: 1. Mai 2010

geschätzte Dauer: 3 years

Bezahlung: BAT 2a/2

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