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J Biol Chem, Vol. 274, Issue 29, 20679-20687, July 16, 1999
From the Pharmaceutical Biotechnology Sector, Biotechnology
Research Institute, Montreal, Quebec H4P 2R2, Canada
Protein-protein interactions play an important
role in the specificity of cellular signaling cascades. By using the
yeast two-hybrid system, a specific interaction was identified between the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E and a novel protein, which was termed ZRP-1 to indicate its
sequence similarity to the Zyxin protein family. The mRNA encoding
this protein is distributed widely in human tissues and contains an
open reading frame of 1428 base pairs, predicting a polypeptide of 476 amino acid residues. The deduced protein displays a proline-rich
amino-terminal region and three double zinc finger LIM domains at its
carboxyl terminus. The specific interaction of this novel protein with
the second PDZ domain of hPTP1E was demonstrated both in
vitro, using bacterially expressed proteins, and in
vivo, by co-immunoprecipitation studies. Deletion analysis
indicated that an intact carboxyl terminus is required for its
interaction with the second PDZ domain of hPTP1E in the yeast
two-hybrid system and suggested that other sequences, including the LIM
domains, also participate in the interaction. The genomic organization
of the ZRP-1 coding sequence is identical to that of the lipoma
preferred partner gene, another Zyxin-related protein, suggesting that
the two genes have evolved from a recent gene duplication event.
ZRP-1, a Zyxin-related Protein, Interacts with the Second PDZ
Domain of the Cytosolic Protein Tyrosine Phosphatase hPTP1E
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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