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The Y’s that bind: negative regulators of Src family kinase activity in platelets
Author(s) -
NEWMAN D. K.
Publication year - 2009
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2009.03369.x
Subject(s) - proto oncogene tyrosine protein kinase src , kinase , src family kinase , tyrosine protein kinase csk , microbiology and biotechnology , platelet activation , tyrosine kinase , protein tyrosine phosphatase , sh3 domain , platelet , phosphatase , phosphorylation , biology , chemistry , signal transduction , immunology
Summary. Members of the Src family of protein tyrosine kinases play important roles in platelet adhesion, activation, and aggregation. The purpose of this review is to summarize current knowledge regarding how Src family kinase activity is regulated in general, to describe what is known about mechanisms underlying SFK activation in platelets, and to discuss platelet proteins that contribute to SFK inactivation, particularly those that use phosphotyrosine‐containing sequences to recruit phosphatases and kinases to sites of SFK activity.