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Monoclonal antibodies against the acetylcholine receptor γ‐subunit as site specific probes for receptor tyrosine phosphorylation
Author(s) -
Tzartos Socrates J.,
Tzartos Elisabeth,
Tzartos John S.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00316-2
Subject(s) - acetylcholine receptor , phosphorylation , monoclonal antibody , epitope , tyrosine phosphorylation , microbiology and biotechnology , tyrosine , nicotinic acetylcholine receptor , chemistry , interleukin 10 receptor, alpha subunit , protein subunit , gamma subunit , biochemistry , receptor , biology , g alpha subunit , antibody , immunology , gene
Tyrosine phosphorylation of the nicotinic acetylcholine receptor (AChR) may be involved in AChR desensitization and clustering. Torpedo AChR γ‐subunit is phosphorylated at Tyr 365 . Using overlapping synthetic peptides, we have precisely mapped the epitopes of five anti‐γ‐subunit monoclonal antibodies (mAbs) and found that the epitope(s) for the mAbs 154, 165 and 168 (γ365–370) all contain Tyr 365 . mAb 168 is a known blocker of AChR channel function. Using peptide analogues, Tyr 365 . was found to be indispensable for mAb165 binding; furthermore its binding was selectively inhibited by in vitro AChR tyrosine phosphorylation. The possible connection between γ‐subunit phosphorylation and regulation of AChR function and the proven usefulness of these mAbs as tools should facilitate functional studies of AChR γ‐subunit phosphorylation.