Ezrin is a substrate for Lck in T cells

FEBS Letters

Rönnstrand, Lars¹  Carpén, Olli³  Vaheri, Antti²  Gahmberg, Carl G⁴  Autero, Matti⁴  Heiska, Leena³ 

[1] Signal Transduction Group, Ludwig Institute for Cancer Research, Uppsala, Sweden;Department of Virology, Haartman Institute, University of Helsinki, Helsinki, Finland;Biomedicum, Neuroscience Program and Department of Pathology, University of Helsinki and HUCH, Helsinki, Finland;Department of Biosciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland

关键词: T lymphocyte;    Lck;    Actin cytoskeleton;    Adhesion;    PTK;    protein tyrosine kinase;    ERM;    ezrin–radixin–moesin;    PTPase;    protein tyrosine phosphatase;   

DOI  :  10.1016/S0014-5793(02)03861-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown