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J Biol Chem. 1999 Jan 22;274(4):2303-7.

Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22.

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  • 1Howard Hughes Medical Institute, Department of Pathology and Molecular Microbiology, Center for Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

Abstract

CD22 phosphorylation is an early event of B cell antigen receptor engagement and results in the recruitment of the negative regulatory tyrosine phosphatase, SHP-1. Peptides representing the potential phosphorylation sites within the cytoplasmic domain of CD22 have been used to stimulate SHP-1 catalytic activity and to inhibit the binding of SHP-1 to CD22 (Doody, G., Justement, L., Delibrias, C., Matthews, R., Lin, J., Thomas, M., and Fearon, D. (1995) Science 269, 242-244). However, the sites of phosphorylation within the cytoplasmic domain of CD22 and the importance of each for the recruitment and activation of SHP-1 remain unknown. Here we demonstrate that there are multiple sites within the cytoplasmic domain of CD22 that interact with the Src homology 2 domains of SHP-1. Nevertheless, a minimum of two tyrosines in CD22 is required for the association with SHP-1. Furthermore, both Src homology 2 domains of SHP-1 are necessary for efficient binding to CD22.

PMID:
9890995
[PubMed - indexed for MEDLINE]
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