Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155393
Author(s) Gesemann, M.; Cavalli, V.; Denzer, A. J.; Brancaccio, A.; Schumacher, B.; Ruegg, M. A.
Author(s) at UniBasel Rüegg, Markus A.
Year 1996
Title Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
Journal Neuron
Volume 16
Number 4
Pages / Article-Number 755-67
Keywords Agrin/chemistry/*genetics/*metabolism; *Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cell Line; Chickens; Cytoskeletal Proteins/*metabolism; Dystroglycans; Heparin/*metabolism; Membrane Glycoproteins/*metabolism; Mice; Molecular Sequence Data; Muscles/metabolism; Receptors; Cholinergic/chemistry/metabolism; Growth Factor/*metabolism
Mesh terms Agrin, metabolism; Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cell Line; Chickens; Cytoskeletal Proteins, metabolism; Dystroglycans; Heparin, metabolism; Membrane Glycoproteins, metabolism; Mice; Molecular Sequence Data; Muscles, metabolism; Receptors, Cholinergic, metabolism; Receptors, Growth Factor, metabolism
Abstract Agrin is a heparan sulfate proteoglycan that induces aggregation of acetylcholine receptors (AChRs) at the neuromuscular synapse. This aggregating activity is modulated by alternative splicing. Here, we compared binding of agrin isoforms to heparin, alpha-dystroglycan, and cultured myotubes. We find that the alternatively spliced 4 amino acids insert (KSRK) is required for heparin binding. The binding affinity of agrin isoforms to alpha-dystroglycan correlates neither with binding to heparin nor with their AChR-aggregating activities. Moreover, the minimal fragment sufficient to induce AChR aggregation does not bind to alpha-dystroglycan. Nevertheless, this fragment still binds to cultured muscle cells. Its binding is completed only by agrin isoforms that are active in AChR aggregation, and therefore this binding site is likely to represent the receptor that initiates AChR clustering.
Publisher Cell Press
ISSN/ISBN 0896-6273
edoc-URL http://edoc.unibas.ch/dok/A5258427
Full Text on edoc Restricted
Digital Object Identifier DOI 10.1016/S0896-6273(00)80096-3
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/8607994
ISI-Number WOS:A1996UG61100009
Document type (ISI) Journal Article
 
   

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