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J. Biol. Chem., Vol. 281, Issue 34, 24721-24727, August 25, 2006

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Regulation of Survivin Stability by the Aryl Hydrocarbon Receptor-interacting Protein^*

From the Department of Cancer Biology and the Cancer Center, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Survivin is a multifunctional member of the IAP (inhibitor of apoptosis) family, but its molecular interactions in protection from cell death and regulation of cell division have not been completely elucidated. In a proteomics screening to identify novel survivin-binding partners, we found that the aryl hydrocarbon receptor-interacting protein (AIP) directly associates with survivin in vitro and in co-immunoprecipitation experiments in vivo. This interaction is mediated by the carboxyl-terminal end of AIP, which contains three tetratricopeptide motifs, and involves the carboxyl terminus coiled coil in survivin with critical roles of Asp¹⁴² in AIP recognition. A survivin mutant lacking only Asp¹⁴² fails to bind AIP and exhibits accelerated degradation in vivo in a reaction reversed by a proteasome inhibitor. Acute knock-down of AIP by short interference RNA or competition of the survivin-AIP complex by peptidyl mimicry destabilizes survivin levels in cells, with enhanced apoptosis but no changes in cell cycle progression. Therefore, AIP regulates survivin stability, thus elevating a cellular anti-apoptotic threshold. The survivin-AIP complex may influence the cellular xenobiotic response to environmental toxin(s) and contribute to subcellular chaperone trafficking during cell death regulation.

Received for publication, April 4, 2006 , and in revised form, May 31, 2006.

^* This work was supported by National Institutes of Health Grants CA90917, CA78810, and HL54131. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by a post-doctoral fellowship program of Korea Science & Engineering Foundation.

² To whom correspondence should be addressed: Dept. of Cancer Biology, LRB428, 364 Plantation St., Worcester, MA 01605. Tel.: 508-856-5775; Fax: 508-856-5792; E-mail: dario.altieri{at}umassmed.edu.

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