The Activated Form of the Lck Tyrosine Protein Kinase in Cells Exposed to Hydrogen Peroxide Is Phosphorylated at Both Tyr-394 and Tyr-505

作者: James S. Hardwick , Bartholomew M. Sefton

DOI: 10.1074/JBC.272.41.25429

关键词:

摘要: Members of the Src family non-receptor tyrosine protein kinases are known to be inhibited by intramolecular association between a phosphorylated carboxyl-terminal residue and SH2 domain. We have previously shown that exposure cells H2O2 strongly activates Lck, lymphocyte-specific kinase, inducing phosphorylation on Tyr-394, an absolutely conserved within activation loop catalytic Here we show Lck has been activated is simultaneously at both (Tyr-505) Tyr-394. Thus, dephosphorylation Tyr-505 not prerequisite for either Tyr-394 or kinase. These results indicate dominant over any inhibition induced Tyr-505. propose these may extended all members.

参考文章(44)
J.P. Secrist, L.A. Burns, L. Karnitz, G.A. Koretzky, R.T. Abraham, Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. Journal of Biological Chemistry. ,vol. 268, pp. 5886- 5893 ,(1993) , 10.1016/S0021-9258(18)53403-7
L.A. Paige, M.J. Nadler, M.L. Harrison, J.M. Cassady, R.L. Geahlen, Reversible palmitoylation of the protein-tyrosine kinase p56lck Journal of Biological Chemistry. ,vol. 268, pp. 8669- 8674 ,(1993) , 10.1016/S0021-9258(18)52927-6
A M Shenoy-Scaria, L K Gauen, J Kwong, A S Shaw, D M Lublin, Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Molecular and Cellular Biology. ,vol. 13, pp. 6385- 6392 ,(1993) , 10.1128/MCB.13.10.6385
L Karnitz, S L Sutor, T Torigoe, J C Reed, M P Bell, D J McKean, P J Leibson, R T Abraham, Effects of p56lck deficiency on the growth and cytolytic effector function of an interleukin-2-dependent cytotoxic T-cell line. Molecular and Cellular Biology. ,vol. 12, pp. 4521- 4530 ,(1992) , 10.1128/MCB.12.10.4521
J D Marth, J A Cooper, C S King, S F Ziegler, D A Tinker, R W Overell, E G Krebs, R M Perlmutter, Neoplastic transformation induced by an activated lymphocyte-specific protein tyrosine kinase (pp56lck). Molecular and Cellular Biology. ,vol. 8, pp. 540- 550 ,(1988) , 10.1128/MCB.8.2.540
André Veillette, Michael A. Bookman, Eva M. Horak, Joseph B. Bolen, The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck Cell. ,vol. 55, pp. 301- 308 ,(1988) , 10.1016/0092-8674(88)90053-0
K. E. Amrein, B. M. Sefton, Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56lck, reveals its oncogenic potential in fibroblasts. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 85, pp. 4247- 4251 ,(1988) , 10.1073/PNAS.85.12.4247