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A more recent version of this article appeared on April 5, 2002
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M110568200v1
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Papers In Press, published online ahead of print January 25, 2002
J. Biol. Chem, 10.1074/jbc.M110568200
Submitted on November 2, 2001
Revised on January 15, 2002
Accepted on January 25, 2002

The mechanism of growth inhibitory effect of DOC-2/DAB2 in prostate cancer: Characterization of a novel GTPase activating protein associated with N-terminal domain of DOC-2/DAB2

Zhi Wang, Ching-Ping Tseng, Rey-Chen Pong, Hong Chen, John D. McConnell, Nora Navone, and Jer-Tsong Hsieh

Urology, J8-144, UT Southwestern Medical Center, Dallas, TX 75235-9110

Corresponding Author: JT.Hsieh{at}UTSouthwestern.edu

DOC-2/DAB2 is a member of the disable gene family with tumor inhibitory activity. Its down regulation is associated with several neoplasms, and serine phosphorylation of its N-terminus modulates DOC-2/DAB2’s inhibitory effect on AP-1 transcriptional activity. We describe the cloning of DIP1/2, a novel gene that interacts with the N-terminal of DOC-2/DAB2. DIP1/2 is a novel GTPase-activating protein containing a Ras GAP homology domain (N-terminus) and two other unique domains (i.e., 10 proline repeats and leucine zipper). Interaction between DOC-2/DAB2 and DIP1/2 is detected in normal tissues such as the brain and prostate. Altered expression of these two proteins is often detected in prostate cancer cells. Indeed, presence of DIP1/2 effectively blocks mitogen-induced gene expression and inhibits the growth of prostate cancer. Thus, DOC-2/DAB2 and DIP1/2 appear to represent a unique negative regulatory complex that maintains cell homeostasis.


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