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- Title
The effects of post-translational processing on dystroglycan synthesis and trafficking<sup>1</sup><FN ID="FN1"><NO>1</NO>EMBL accession number AJ584830.</FN>
- Authors
Esapa, Chris T.; Bentham, Graham R.B.; Schröder, Jörn E.; Kröger, Stephan; Blake, Derek J.
- Abstract
Dystroglycan is a component of the dystrophin glycoprotein complex that is cleaved into two polypeptides by an unidentified protease. To determine the role of post-translational processing on dystroglycan synthesis and trafficking we expressed the dystroglycan precursor and mutants thereof in a heterologous system. A point mutant in the processing site, S655A, prevented proteolytic cleavage but had no effect upon the surface localisation of dystroglycan. Mutation of two N-linked glycosylation sites that flank the cleavage site inhibited proteolytic processing of the precursor. Furthermore, chemical inhibition of N- and O-linked glycosylation interfered with the processing of the precursor and reduced the levels of dystroglycan at the cell surface. Dystroglycan processing was also inhibited by the proteasome inhibitor lactacystin. N-linked glycosylation is a prerequisite for efficient proteolytic processing and cleavage and glycosylation are dispensable for cell surface targeting of dystroglycan.
- Subjects
DYSTROPHIN; GLYCOPROTEINS; PEPTIDES; GLYCOSYLATION
- Publication
FEBS Letters, 2003, Vol 555, Issue 2, p209
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)01230-4