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M011562200v1
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Papers In Press, published online ahead of print January 22, 2001
J. Biol. Chem, 10.1074/jbc.M011562200
Submitted on December 21, 2000
Revised on January 12, 2001
Accepted on January 22, 2001

ATF-7, a novel bZIP protein, interacts with the PRL-1 PTPase

Charles S. Peters, Xianping Liang, Shuixing Li, Yong Peng, Rebecca Taub, and Robert H. Diamond

Department of Medicine/GI Division, University of Pennsylvania School of Medicine, Philadelphia, PA 19104

Corresponding Author: diamondr{at}mail.med.upenn.edu

We have identified a novel basic leucine zipper (bZIP) protein, designated ATF-7 that physically interacts with the PRL-1 protein tyrosine phosphatase (PTPase). PRL-1 is a predominantly nuclear, farnesylated PTPase that has been linked to the control of cellular growth and differentiation. This interaction was initially found using the yeast two-hybrid system. ATF-7 is most closely related to members of the ATF/CREB family of bZIP proteins, with highest homology to ATF-4. ATF-7 homodimers can bind specifically to CRE elements. ATF-7 is expressed in a number of different tissues, and is expressed in association with differentiation in the Caco-2 cell model of intestinal differentiation. We have confirmed the PRL-1/ATF-7 interaction and mapped the regions of ATF-7 and PRL-1 important for interaction to ATF-7?s bZIP region and PRL-1?s phosphatase domain. Finally, we have determined that PRL-1 is able to dephosphorylate ATF-7 in vitro. Further insight into ATF-7?s precise cellular roles, transcriptional function and downstream targets are likely be of importance in understanding the mechanisms underlying the complex processes of maintenance, differentiation and turnover of epithelial tissues.


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