p56LCK Phosphorylation by Ca2+/Calmodulin-Dependent Protein-Kinase Type II
| Autor: | O.B. Mcdonald, M.M. Bland, A.C. Carrera |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Male
Phosphopeptides T-Lymphocytes Immunoblotting Biophysics Mitogen-activated protein kinase kinase Biology Peptide Mapping Biochemistry Rats Sprague-Dawley Prosencephalon Ca2+/calmodulin-dependent protein kinase Animals c-Raf Phosphorylation Protein kinase A Egtazic Acid Molecular Biology Serine/threonine-specific protein kinase hemic and immune systems Cell Biology Protein-Tyrosine Kinases Molecular biology Rats Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Calcium-Calmodulin-Dependent Protein Kinases Electrophoresis Polyacrylamide Gel cGMP-dependent protein kinase Tyrosine kinase Signal Transduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 198:67-73 |
| ISSN: | 0006-291X |
| Popis: | Ca 2+ /calmodulin-dependent protein kinases are implicated in regulating the Ca 2+ signaling involved in T cell activation and in thymocyte selection. One of the earliest events in signaling through the T cell antigen receptor is activation of the protein tyrosine kinase p56lck. Following T cell activation or signaling through the IL-2 receptor, Ca 2+ -mediated phosphorylation of p56lck occurs on serine/threonine residues. Isoforrns of the multifunctional Ca 2+ /calmodulin-dependent protein kinases, CaM kinase-II and CaM kinase-Gr are found in human T lymphocytes. CaM kinase-II, but not CaM kinase-Gr, phosphorylates the T cell tyrosine kinase p56lck in vitro . Tryptic phosphopeptide maps indicate that CaM kinase-II phosphorylates p56lck on multiple sites in vitro . Kinase assays of p56lck modified by CaM kinase-II indicate that CaM kinase-II modification does not appreciably affect p56lck phosphotransfer activity. |
| Databáze: | OpenAIRE |
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