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Papers In Press, published online ahead of print December 20, 2001
Medicine, Vanderbilt University, Nashville, TN 37232
Corresponding Author: joe.zhao{at}mcmail.vanderbilt.edu
PZR is an immunoglobulin superfamily cell surface protein containing a pair of immuno-receptor tyrosine-based inhibitory motifs. As a glycoprotein, PZR displayed a strong association with concanavalin A (Con A), a member of the plant lectin family. Treatment of several cell lines with Con A caused tyrosine phosphorylation of a major cellular protein. Immunoblotting and immunoprecipitation studies indicated that this protein corresponded to PZR. Tyrosine phosphorylation of PZR was accompanied by recruitment of SHP-2 and was inhibited by PP1, a selective inhibitor of the Src family tyrosine kinases. Furthermore, c-Src was constitutively associated with PZR and was activated upon treatment of cells with Con A. Moreover, tyrosine phosphorylation of PZR was markedly enhanced in v-Src-transformed NIH 3T3 cells and was predominant in E. coli cells co-expressing c-Src. Expression of an intracellular domain-truncated form of PZR in HT-1080 cells affected cell morphology and had a dominant negative effect on Con A-induced tyrosine phosphorylation of PZR, activation of c-Src, and agglutination of the cells. Together, the data indicate that PZR is a major receptor of Con A and has an important role in cell signaling via c-Src. Considering the various biological activities of Con A, the study of PZR may have major therapeutic implications.
J. Biol. Chem, 10.1074/jbc.M111914200
Submitted on December 14, 2001
Revised on December 20, 2001
Accepted on December 20, 2001
Cell surface glycoprotein PZR is a major mediator of concanavalin A-induced cell signaling
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