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• W2062135534 startingPage "644" @default.
• W2062135534 abstract "Despite the important role in the development and activation of T cells, NK cells, mast cells, and macrophages, the expression and function of SLP-76 in B cells have been largely unknown. Here we demonstrate that SLP-76 is expressed in all mouse B cell lines tested and in normal splenic B cells, and serves as an SHP-1 substrate. Dephosphorylation of SLP-76 by SHP-1 inhibits its association with Nck, down-regulating c-Jun N-terminal kinase (JNK) activation and exerting a positive effect on apoptosis. Knockdown of SLP-76 in WEHI-231 cells by small interfering RNA attenuated JNK activation, but showed little effects on extracellular signal-regulated kinase (ERK) or p38 activation. Although WEHI-231 does not express linker for activation of T cells (LAT), SLP-76 localizes in membrane fraction, which increases following B cell receptor (BCR) cross-linking. Further analyses revealed that SLP-76 complexed with Gads is associated with tyrosine-phosphorylated CD22 through the SH2 domains of SLP-76 and Gads. Given that SHP-1 binds to CD22 upon BCR ligation, our findings suggest that dephosphorylation of SLP-76 recruited to CD22 by SHP-1 inhibits BCR-induced JNK activation, dictating apoptosis." @default.
• W2062135534 created "2016-06-24" @default.
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• W2062135534 date "2005-02-01" @default.
• W2062135534 modified "2023-09-27" @default.
• W2062135534 title "SLP-76 is recruited to CD22 and dephosphorylated by SHP-1, thereby regulating B?cell receptor-induced c-Jun N-terminal kinase activation" @default.
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• W2062135534 doi "https://doi.org/10.1002/eji.200425465" @default.
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• W2062135534 hasPublicationYear "2005" @default.
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