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FEBS Lett. 1998 Dec 28;441(3):357-60.

Tyrosine phosphorylation and translocation of LAT in platelets.

Author information

1
Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill 27599-7525, USA. sarkarf@med.unc.edu

Abstract

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 beta3, translocates to the cytoskeleton during the late stage of thrombin-stimulated irreversible aggregation and not during ADP-stimulated reversible aggregation.

PMID:
9891970
DOI:
10.1016/s0014-5793(98)01584-1
[Indexed for MEDLINE]
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