The effects of post-translational processing on dystroglycan synthesis and trafficking

Esapa, Chris T., Bentham, Graham R. B., Schröder, Jörn E., Kröger, Stephan and Blake, Derek J. ORCID: https://orcid.org/0000-0002-5005-4731 2003. The effects of post-translational processing on dystroglycan synthesis and trafficking. FEBS Letters 555 (2) , pp. 209-216. 10.1016/S0014-5793(03)01230-4

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	MRC Centre for Neuropsychiatric Genetics and Genomics (CNGG) Medicine
Subjects:	R Medicine > R Medicine (General)
Uncontrolled Keywords:	dystroglycan, processing, mucin, glycosylation, proteasome inhibitor
Publisher:	Elsevier
ISSN:	0014-5793
Last Modified:	24 Oct 2022 11:36
URI:	https://orca.cardiff.ac.uk/id/eprint/48687

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