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• W2032189192 endingPage "1392" @default.
• W2032189192 startingPage "1387" @default.
• W2032189192 abstract "The 75-kD HS1 protein is highly tyrosine-phosphorylated during B cell antigen receptor (BCR)-mediated signaling. Owing to low expression of HS1, WEHI-231-derived M1 cells, unlike the parental cells, are insensitive to BCR-mediated apoptosis. Here, we show that BCR-associated tyrosine kinases Lyn and Syk synergistically phosphorylate HS1, and that Tyr378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. In addition, unlike wild-type HS1, a mutant HS1 carrying the mutations Phe-378 and Phe-397 was unable to render M1 cells sensitive to apoptosis. Wild-type HS1, but not the mutant, localized to the nucleus under the synergy of Lyn and Syk. Thus, tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis." @default.
• W2032189192 created "2016-06-24" @default.
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• W2032189192 date "1997-04-07" @default.
• W2032189192 modified "2023-09-30" @default.
• W2032189192 title "Role of Tyrosine Phosphorylation of HS1 in B Cell Antigen Receptor-mediated Apoptosis" @default.
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• W2032189192 doi "https://doi.org/10.1084/jem.185.7.1387" @default.
• W2032189192 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2196252" @default.
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