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Induction of phosphotyrosine in the gap junction protein, connexin43 1
Author(s) -
Mikalsen Svein-Ole,
Husøy Trine,
Vikhamar Gunnhild,
Sanner Tore
Publication year - 1997
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/s0014-5793(96)01489-5
Subject(s) - phosphorylation , protein tyrosine phosphatase , tyrosine phosphorylation , tyrosine , sh2 domain , chemistry , protein phosphorylation , phosphatase , microbiology and biotechnology , biology , biochemistry , protein kinase a
The protein‐tyrosine phosphatase inhibitors pervanadate, permolybdate, H 2 O 2 , and to a much lesser extent vanadate, increased the amount of cellular phosphotyrosine and induced tyrosine phosphorylation of connexin43 (Cx43) in early passage hamster embryo fibroblasts. The presence of phosphotyrosine in Cx43 immunoprecipitates from pervanadate‐treated cells was shown by a phosphotyrosine‐specific antibody and a phosphotyrosine‐specific phosphatase. Pervanadate‐induced Cx43 tyrosine phosphorylation was further verified by phosphoamino acid analysis, while no phosphotyrosine was present in control cells. This is the first observation of tyrosine phosphorylation of connexins in normal cells.