Format

Send to

Choose Destination
FEBS Lett. 2003 Jan 30;535(1-3):82-6.

Ezrin is a substrate for Lck in T cells.

Author information

1
Department of Biosciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland.

Abstract

We evaluated the role of Lck tyrosine kinase, an early effector of T cell activation, in regulation of the membrane-cytoskeleton linker protein ezrin. Ezrin was constitutively tyrosine phosphorylated in wild-type and CD45-deficient Jurkat T cells, but not in Lck-deficient cells. However, phosphorylation was evident in cells, in which Lck activity had been restored by transfection. Phosphorylation was reduced by the Src family kinase inhibitor PP2 and increased by the tyrosine phosphatase inhibitor pervanadate, implying continuous tyrosine phosphorylation and dephosphorylation. Lck phosphorylated ezrin in vitro, and the major phosphotyrosine was identified as Y145. These results identify ezrin as the first cytoskeletal substrate for Lck.

PMID:
12560083
DOI:
10.1016/s0014-5793(02)03861-9
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center