Ezrin is a substrate for Lck in T cells

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, phosphoryla...

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Bibliographic Details
Published in:FEBS letters 2003-01, Vol.535 (1-3), p.82-86
Main Authors: Autero, Matti, Heiska, Leena, Rönnstrand, Lars, Vaheri, Antti, Gahmberg, Carl G, Carpén, Olli
Format: Article
Language:English
Subjects:
Actin cytoskeleton
Adhesion
Cell Line
Cytoskeletal Proteins
Enzyme Inhibitors - pharmacology
ERM, ezrin–radixin–moesin
Humans
Immunoblotting
Jurkat Cells
Lck
Leukocyte Common Antigens - biosynthesis
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - antagonists & inhibitors
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - deficiency
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - genetics
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/antagonists & inhibitors/deficiency/genetics/metabolism
Peptide Mapping
Phosphoproteins - chemistry
Phosphoproteins - genetics
Phosphoproteins - metabolism
Phosphoproteins/chemistry/genetics/metabolism
Phosphorylation - drug effects
PTK, protein tyrosine kinase
PTPase, protein tyrosine phosphatase
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Recombinant Fusion Proteins/genetics/metabolism
T lymphocyte
T-Lymphocytes - drug effects
T-Lymphocytes - metabolism
T-Lymphocytes/drug effects/metabolism
Transfection
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)03861-9