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Publication Detail
The B-cell transmembrane protein CD72 binds to and is an in vivo substrate of the protein tyrosine phosphatase SHP-1
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Article
  • Authors:
    Wu Y, Nadler MJ, Brennan LA, Gish GD, Timms JF, Fusaki N, Jongstra_Bilen J, Tada N, Pawson T, Wither J, Neel BG, Hozumi N
  • Publication date:
    1998
  • Pagination:
    1009, 17
  • Journal:
    Current Biology
  • Volume:
    8
  • Issue:
    18
  • Status:
    Published
  • Print ISSN:
    0960-9822
  • Keywords:
    Apoptosis, Mice, Molecular Biology, OnCite, Ontario, Phosphorylation, Protein-Tyrosine-Phosphatase, Role
  • Notes:
    Program in Molecular Biology, Mount Sinai Hospital, University of Toronto, Ontario, Canada.Alternate Journal: Curr Biol
Abstract
BACKGROUND: Signals from the B-cell antigen receptor (BCR) help to determine B-cell fate, directing either proliferation, differentiation, or growth arrest/apoptosis. The protein tyrosine phosphatase SHP-1 is known to regulate the strength of BCR signaling. Although the B-cell co-receptor CD22 binds SHP-1, B cells in CD22-deficient mice are much less severely affected than those in SHP-1-deficient mice, suggesting that SHP-1 may also regulate B-cell signaling by affecting other signaling molecules. Moreover, direct substrates of SHP-1 have not been identified in any B-cell signaling pathway. RESULTS: We identified the B-cell transmembrane protein CD72 as a new SHP-1 binding protein and as an in vivo substrate of SHP-1 in B cells. We also defined the binding sites for SHP-1 and the adaptor protein Grb2 on CD72. Tyrosine phosphorylation of CD72 correlated strongly with BCR-induced growth arrest/apoptosis in B-cell lines and in primary B cells. Preligation of CD72 attenuated BCR-induced growth arrest/death signals in immature and mature B cells or B-cell lines, whereas preligation of CD22 enhanced BCR-induced growth arrest/apoptosis. CONCLUSIONS: We have identified CD72 as the first clear in vivo substrate of SHP-1 in B cells. Our results suggest that tyrosine-phosphorylated CD72 may transmit signals for BCR-induced apoptosis. By dephosphorylation CD72. SHP-1 may have a positive role in B-cell signaling. These results have potentially important implications for the involvement of CD72 and SHP-1 in B-cell development and autoimmunity.
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