Ezrin is a substrate for Lck in T cells

被引:37
作者
Autero, M
Heiska, L
Rönnstrand, L
Vaheri, A
Gahmberg, CG
Carpén, O [1 ]
机构
[1] Univ Helsinki, Div Biochem, Dept Biosci, Helsinki, Finland
[2] Univ Helsinki, Biomedicum, Program Neurosci, Helsinki, Finland
[3] Univ Helsinki, Dept Pathol, Helsinki, Finland
[4] HUCH, Helsinki, Finland
[5] Ludwig Inst Canc Res, Signal Signal Grp, S-75124 Uppsala, Sweden
[6] Univ Helsinki, Haartman Inst, Dept Virol, Helsinki, Finland
关键词
T lymphocyte; Lck; actin cytoskeleton; adhesion;
D O I
10.1016/S0014-5793(02)03861-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:82 / 86
页数:5
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