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Platelet talin is phosphorylated by calyculin A
Author(s) -
Murata Kohei,
Sakon Masato,
Kambayashi Junichi,
Okuyama Masaki,
Hase Toshiharu,
Mori Takesada
Publication year - 1995
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240570112
Subject(s) - okadaic acid , phosphorylation , dephosphorylation , phosphatase , microbiology and biotechnology , platelet , chemistry , protein phosphorylation , cytoskeleton , clot retraction , protein kinase c , threonine , biochemistry , thrombin , protein kinase a , biology , cell , serine , immunology
Calyculin A and okadaic acid, potent and cell permeable inhibitors of type 1 and type 2A protein phosphatases, inhibit platelet aggregation and secretion. However, the relationship between phosphatase inhibition and inhibition of platelet function is not well understood. We found that in unstimulated platelets, talin (P235) was phosphorylated at threonine residues by calyculin A. Furthermore, the extent of talin phosphorylation by calyculin A was closely correlated with its inhibition of thrombin‐induced platelet aggregation. Since the binding of talin to platelet glycoprotein IIb/IIIa complex has been shown to be affected by its phosphorylation, these results suggest that type 1 and/or type 2A protein phosphatases may play a role in the regulation of membrane‐cytoskeleton interaction through dephosphorylation of talin.