AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycan
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155395
Author(s) Meier, T.; Gesemann, M.; Cavalli, V.; Ruegg, M. A.; Wallace, B. G.
Author(s) at UniBasel Rüegg, Markus A.
Year 1996
Title AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycan
Journal The EMBO Journal
Volume 15
Number 11
Pages / Article-Number 2625-31
Keywords acetylcholine receptor, agrin, dystroglycan, neuromuscular junction, protein tyrosine phosphorylation
Mesh terms Agrin, metabolism; Animals; Cells, Cultured; Chickens; Cytoskeletal Proteins, metabolism; Dystroglycans; Macromolecular Substances; Membrane Glycoproteins, metabolism; Mice; Muscle, Skeletal, metabolism; Phosphorylation; Phosphotyrosine, metabolism; Protein Binding; Receptor Aggregation; Receptors, Nicotinic, metabolism
Abstract Agrin induces both phosphorylation and aggregation of nicotinic acetylcholine receptors (AChRs) when added to myotubes in culture, apparently by binding to a specific receptor on the myotube surface. One such agrin receptor is alpha-dystroglycan, although binding to alpha-dystroglycan appears not to mediate AChR aggregation. To determine whether agrin-induced AChR phosphorylation is mediated by alpha-dystroglycan or by a different agrin receptor, fragments of recombinant agrin that differ in affinity for alpha-dystroglycan were examined for their ability to induce AChR phosphorylation and aggregation in mouse C2 myotubes. The carboxy-terminal 95 kDa agrin fragment agrin-c95(A0B0), which binds to alpha-dystroglycan with high affinity, failed to induce AChR phosphorylation and aggregation. In contrast, agrin-c95(A4B8) which binds less strongly to alpha-dystroglycan, induced both phosphorylation and aggregation, as did a small 21 kDa fragment of agrin, agrin-c21(B8), that completely lacks the binding domain for alpha-dystroglycan. We conclude that agrin-induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha-dystroglycan.
Publisher Nature Publishing Group
ISSN/ISBN 0261-4189 ; 1460-2075
URL https://www.ncbi.nlm.nih.gov/pmc/articles/PMC450197/
edoc-URL http://edoc.unibas.ch/dok/A5258429
Full Text on edoc Restricted
Digital Object Identifier DOI 10.1002/j.1460-2075.1996.tb00622.x
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/8654359
ISI-Number WOS:A1996UQ62000002
Document type (ISI) Journal Article
 
   

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