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J. Biol. Chem., Vol. 277, Issue 10, 7882-7888, March 8, 2002
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,,¶
From the 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.
Division of Hematology/Oncology, Department
of Medicine, Vanderbilt-Ingram Cancer Center, Vanderbilt University,
Nashville, Tennessee 37232-6307 and the § Department of
Biochemistry, The University of Texas Health Center, Tyler, Texas
75708
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