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Originally published In Press as doi:10.1074/jbc.M200955200 on May 16, 2002

J. Biol. Chem., Vol. 277, Issue 31, 27706-27715, August 2, 2002
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The Human SNF5/INI1 Protein Facilitates the Function of the Growth Arrest and DNA Damage-inducible Protein (GADD34) and Modulates GADD34-bound Protein Phosphatase-1 Activity*

Daniel Y. WuDagger §, Douglas C. Tkachuck||**, Rachel S. RobersonDagger , and William H. SchubachDagger §

From the Dagger  Division of Medical Oncology, Department of Medicine, and the || Department of Pathology, Veterans Administration Puget Sound Health Care System, Seattle Division, Seattle, Washington 98108 and the § Division of Medical Oncology, Department of Medicine, and the ** Department of Pathology, University of Washington Medical Center, Seattle, Washington 98195

The growth arrest and DNA damage-inducible protein (GADD34) mediates growth arrest and apoptosis in response to DNA damage, negative growth signals, and protein malfolding. GADD34 binds to protein phosphatase-1 (PP1) and can attenuate translational elongation of key transcriptional factors through dephosphorylation of eukaryotic initiation factor-2alpha . We reported previously that the human trithorax leukemia fusion protein (HRX) can bind to GADD34 and abrogate GADD34-mediated apoptosis in response to UV irradiation. We found that hSNF5/INI1, a component of the hSWI/SNF chromatin remodeling complex, also binds to GADD34 and can coexist with GADD34 and HRX fusion proteins as a trimolecular complexes in vivo. In the present report, we demonstrate that hSNF5/INI1 binds to GADD34 in part through the PP1 docking site within a domain homologous to herpes simplex virus-1 ICP34.5. We found that hSNF5/INI1 can bind PP1 independently and weakly stimulate its phosphatase activity in solution and in complex with GADD34. hSNF5/INI1 and PP1 do not compete for binding to GADD34 but rather form a stable heterotrimeric complex with GADD34. We also show that Epstein-Barr nuclear protein 2, which binds hSNF5/INI1, can disrupt hSNF5/INI1 binding to GADD34 and partially reverse the GADD34-mediated growth suppression function in Ha-ras expressing HIH-3T3 (3T3-ras) cells. These results implicate hSNF5/INI1 in the function of GADD34 and suggest that hSNF5/INI1 may regulate PP1 activity in vivo.

* This work was supported by the Department of Veteran Affairs (VA Merit Review) and National Institutes of Health Grant 5K08CA71928-01 (to D. Y. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: 111-ONC, Division of Oncology, Veterans Administration Puget Sound Health Care System, Seattle Division, 1660 S. Columbian Way, Seattle, WA 98108. E-mail: danielw@u.washington.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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