Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling.
作者： T Kurosaki , S A Johnson , L Pao , K Sada , H Yamamura
关键词: Signal transduction 、 Immunoreceptor tyrosine-based activation motif 、 Phosphorylation 、 Biology 、 Molecular biology 、 SH2 domain 、 Tyrosine phosphorylation 、 Autophosphorylation 、 Syk 、 Tyrosine kinase
摘要: To explore the mechanism(s) by which Syk protein tyrosine kinase participates in B cell antigen receptor (BCR) signaling, we have studied function of various mutants cells made deficient homologous recombination knockout. Both SH2 domains were required for BCR-mediated and phospholipase C (PLC)-gamma 2 phosphorylation, inositol 1,4,5-triphosphate release, Ca2+ mobilization. A possible explanation this requirement was provided findings that recruitment to tyrosine-phosphorylated immunoglobulin (Ig) alpha Ig beta requires both domains. mutant putative autophosphorylation site (Y518/Y519) changed phenylalanine also defective signal transduction; however, mutation did not affect phosphorylated immunoreceptor family tyrosine-based activation motifs (ITAMs). These only confirm are necessary binding but indicate is (Y518/519) phosphorylation after BCR ligation. This sequence events apparently coupling most cellular PLC-gamma 2,
rupress.org
jem.org参考文章(14)
L.E. Samelson, R.D. Klausner, Tyrosine kinases and tyrosine-based activation motifs. Current research on activation via the T cell antigen receptor. Journal of Biological Chemistry. ,vol. 267, pp. 24913- 24916 ,(1992) , 10.1016/S0021-9258(19)73981-7
M. Reth, E. Petrac, P. Wiese, L. Lobel, F. W. Alt, Activation of V kappa gene rearrangement in pre-B cells follows the expression of membrane-bound immunoglobulin heavy chains. The EMBO Journal. ,vol. 6, pp. 3299- 3305 ,(1987) , 10.1002/J.1460-2075.1987.TB02649.X
J.E. Hutchcroft, M.L. Harrison, R.L. Geahlen, Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor. Journal of Biological Chemistry. ,vol. 267, pp. 8613- 8619 ,(1992) , 10.1016/S0021-9258(18)42487-8
M. A. Campbell, B. M. Sefton, Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin. The EMBO Journal. ,vol. 9, pp. 2125- 2131 ,(1990) , 10.1002/J.1460-2075.1990.TB07381.X
C L Chen, J E Lehmeyer, M D Cooper, Evidence for an IgD homologue on chicken lymphocytes. Journal of Immunology. ,vol. 129, pp. 2580- 2585 ,(1982)
John C. Cambier, New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL) Immunology Today. ,vol. 16, pp. 110- ,(1995) , 10.1016/0167-5699(95)80105-7
M Iwashima, B. Irving, N. van Oers, A. Chan, A Weiss, Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases Science. ,vol. 263, pp. 1136- 1139 ,(1994) , 10.1126/SCIENCE.7509083
C. Koch, D Anderson, M. Moran, C Ellis, T Pawson, SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. ,vol. 252, pp. 668- 674 ,(1991) , 10.1126/SCIENCE.1708916
Takechiyo YAMADA, Takanobu TANIGUCHI, Cheng YANG, Satoshi YASUE, Hitoshi SAITO, Hirohei YAMAMURA, Association with B-cell-antigen receptor with protein-tyrosine kinase p72syk and activation by engagement of membrane IgM FEBS Journal. ,vol. 213, pp. 455- 459 ,(1993) , 10.1111/J.1432-1033.1993.TB17781.X
Andrew C. Chan, Makio Iwashima, Christoph W. Turck, Arthur Weiss, ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain Cell. ,vol. 71, pp. 649- 662 ,(1992) , 10.1016/0092-8674(92)90598-7