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- W4313333857 abstract "Abstract Accumulating evidence indicates that the Src homology 2-containing tyrosine phosphatase 2 (SHP-2) plays an important role in signal transduction through receptor tyrosine kinase and cytokine receptors. In most models, SHP-2 appears to be a positive mediator of signaling. However, coligation of FcγRIIB1 with B cell Ag receptors (BCR) inhibits BCR-mediated signaling by a mechanism that may involve recruitment of phosphatases SHP-1, SHP-2, and the SH2 containing inositol 5′phosphatase (SHIP) to the phosphorylated FcγRIIB1 immunoreceptor tyrosine-based inhibitory motif. The role of SHP-2 in BCR-mediated cell activation and in FcγRIIB1-mediated inhibitory signaling is unclear. In this study we assessed the association of SHP-2 with phosphotyrosine-containing cellular protein(s) before and after stimulation through these receptors. BCR stimulation induced the association of SHP-2 with a single major tyrosyl-phosphorylated molecule (pp120) that had an apparent molecular mass of 120 kDa. Coligation of FcγRIIB1 with BCR led to a rapid decrease in SHP-2 association with pp120. Analysis of the subcellular localization of pp120 showed that the complex of SHP-2 and tyrosyl-phosphorylated p120 occurs predominantly in the cytosol. Furthermore, the binding of the two molecules was mediated by the interaction of tyrosyl-phosphorylated p120 with the SHP-2 N-terminal SH2 domain. These findings indicate that SHP-2 and pp120 function in BCR signaling, and this function may be inhibited by FcγRIIB1 signaling." @default.
- W4313333857 created "2023-01-06" @default.
- W4313333857 creator A5043895289 @default.
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- W4313333857 date "1998-07-15" @default.
- W4313333857 modified "2023-10-16" @default.
- W4313333857 title "B Cell Antigen Receptor (BCR)-Mediated Formation of a SHP-2-pp120 Complex and Its Inhibition by FeγRIIB1-BCR Coligation" @default.
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- W4313333857 doi "https://doi.org/10.4049/jimmunol.161.2.684" @default.
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