Anti-CD3 and phorbol ester induce distinct phosphorylated sites in the SH2 domain of p56lck.
作者： M Soula , B Rothhut , L Camoin , J L Guillaume , D Strosberg
DOI: 10.1016/S0021-9258(19)74265-3
关键词:
摘要: P56lck is a protein tyrosine kinase of the Src family specifically expressed in T lymphocytes. Triggering cells with anti-CD3 or phorbol 12-myristate 13-acetate (PMA) results appearance slower migrating forms (shift) p56lck. To investigate phosphorylation sites on shifted p56lck and to assess role C this phosphorylation, Jurkat were treated selective inhibitor (GF 109203X). This completely reversed shift induced by PMA but only partially one after triggering anti-CD3. analyze further, was immunoprecipitated from vivo labeled either PMA. Tryptic phosphopeptides generated analyzed using combination thin layer chromatography, high reticulation polyacrylamide gel electrophoresis, reverse phase phosphopeptide sequencing. We identified serine 158 as newly phosphorylated site treatment 192 194 major tryptic obtained triggering. The three are located SH2 domain p56lck; suggests that their may regulate interaction other proteins internal domains
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