SHP-1 dephosphorylates 3BP2 and potentially downregulates 3BP2-mediated T cell antigen receptor signaling

DOIResolve DOI: http://doi.org/10.1111/j.1742-4658.2006.05233.x
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TypeArticle
Volume273
Issue10
Pages21952205; # of pages: 11
SubjectCells; pha; phosphatase; Phosphorylation; Protein; Tyrosine
AbstractSrc homology 2 (SH2) domain-containing protein tyrosine phosphatase-1 (SHP -1) is a critical inhibitory regulator in T cell-receptor (TCR) signaling. However, the exact molecular mechanism underlying this is poorly defined, largely because the physiological substrates for SHP-1 in T cells remain elusive. In this study, we showed that adaptor protein 3BP2 serves as a binding protein and a physiological substrate of SHP-1. 3BP2 is phosphorylated on tyrosyl residue 448 in response to TCR activation, and the phosphorylation is required for T cell signalling, as indicated by transcriptional activation of nuclear factor activated in T cells (NFAT). Concurrently, phosphorylation of Tyr566 at the C-terminus of SHP-1 causes specific recruitment of 3BP2 to the phosphatase through the SH2 domain of the adaptor protein. This leads to efficient dephosphorylation of 3BP2 and thereby termination of T cell signaling. The study thus defines a novel function of the C-terminal segment of SHP-1 and reveals a new mechanism by which T cell signaling is regulated
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47506
NPARC number3539390
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Record identifier398ef5dc-aa41-42b9-9a70-c2293f546233
Record created2009-03-01
Record modified2016-05-09
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