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J. Biol. Chem. Mar (2002); 277(10):7882-8
Cell surface glycoprotein PZR is a major mediator of concanavalin A-induced cell signaling.
Zhao R, Guerrah A, Tang H, Zhao ZJ
Division of Hematology/Oncology, Department of Medicine, Vanderbilt-Ingram Cancer Center, Vanderbilt University, Nashville, Tennessee 37232-6307, USA.
Abstract: PZR is an immunoglobulin superfamily cell surface protein containing a pair of immunoreceptor tyrosine-based inhibitory motifs. As a glycoprotein, PZR displays a strong association with concanavalin A (ConA), a member of the plant lectin family. Treatment of several cell lines with ConA 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 ConA. Moreover, tyrosine phosphorylation of PZR was markedly enhanced in v-Src-transformed NIH-3T3 cells and was predominant in Escherichia 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 ConA-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 ConA and has an important role in cell signaling via c-Src. Considering the various biological activities of ConA, the study of PZR may have major therapeutic implications.
[PUBMED: 11751924] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.