Premium
Tyrosine phosphorylation and translocation of LAT in platelets
Author(s) -
Sarkar Sibaji
Publication year - 1998
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(98)01584-1
Subject(s) - syk , tyrosine phosphorylation , phosphorylation , tyrosine , thrombin , platelet , chemistry , microbiology and biotechnology , cytoskeleton , tyrosine kinase , protein tyrosine phosphatase , chromosomal translocation , platelet aggregation , protein phosphorylation , biochemistry , biology , cell , signal transduction , protein kinase a , immunology , gene
Platelet aggregation is accompanied by the tyrosine phosphorylation of several proteins including syk. However, some of these proteins are not identified. Recent studies showed that LAT is a syk substrate and is tyrosine phosphorylated during T cell stimulation. In this study, we demonstrated that LAT is present in platelets and is tyrosine phosphorylated in response to ADP‐ and thrombin‐stimulated aggregation. Moreover, LAT, like syk and β 3 , translocates to the cytoskeleton during the late stage of thrombin‐stimulated irreversible aggregation and not during ADP‐stimulated reversible aggregation.