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Ezrin is a substrate for Lck in T cells
Author(s) -
Autero Matti,
Heiska Leena,
Rönnstrand Lars,
Vaheri Antti,
Gahmberg Carl G,
Carpén Olli
Publication year - 2003
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(02)03861-9
Subject(s) - ezrin , phosphorylation , dephosphorylation , tyrosine phosphorylation , microbiology and biotechnology , protein tyrosine phosphatase , jurkat cells , tyrosine , proto oncogene tyrosine protein kinase src , chemistry , cytoskeleton , tyrosine protein kinase csk , tyrosine kinase , kinase , cancer research , phosphatase , biology , signal transduction , sh2 domain , t cell , cell , biochemistry , immunology , immune system
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.