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J. Biol. Chem., Vol. 280, Issue 7, 5468-5474, February 18, 2005

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ASB2 Is an Elongin BC-interacting Protein That Can Assemble with Cullin 5 and Rbx1 to Reconstitute an E3 Ubiquitin Ligase Complex^*

Mélina L. Heuzé, Florence C. Guibal¶, Charles A. Banks||, Joan W. Conaway||, Ronald C. Conaway||, Yvon E. Cayre**, Arndt Benecke¶¶, and Pierre G. Lutz||||

From the INSERM, U417, Hôpital Robert Debré, 48 Boulevard Serurier, F-75935 Paris Cedex 19, France, ^||Stowers Institute for Medical Research, Kansas City, Missouri 64110, ^**Department of Microbiology/Immunology, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107-5541, University La Sapienza II, Roma 00161, Italy, and Institut des Hautes Etudes Scientifiques, 35 route de Chartres, F-91440 Bures-sur-Yvette, France

The ankyrin repeat-containing protein with a suppressor of cytokine signaling box-2 (ASB2) gene was identified as a retinoic acid-response gene and a target of the promyelocytic leukemia-retinoic acid receptor- oncogenic protein characteristic of acute promyelocytic leukemia. Expression of ASB2 in myeloid leukemia cells inhibits growth and promotes commitment, recapitulating an early step known to be critical for differentiation. Here we show that ASB2, by interacting with the Elongin BC complex, can assemble with Cullin5·Rbx1 to form an E3 ubiquitin ligase complex that stimulates polyubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. This is a first indication that a member of the ASB protein family, ASB2, is a subunit of an ECS (Elongin C-Cullin-SOCS box)-type E3 ubiquitin ligase complex. Altogether, our results strongly suggest that ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate.

Received for publication, November 18, 2004

^* This work was supported by INSERM, by the CNRS, and by grants from the Fondation de France (to P. L.). 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.

Present address: Département de Biologie Cellulaire, Institut Cochin, INSERM, U567, CNRS, UMR8104, Univ. Paris V, F-75014 Paris, France.

^¶ Supported by the Ligue Nationale contre le Cancer, by the Société Française d'Hématologie, and by the European Molecular Biology Organization (a European Molecular Biology Organization short term fellowship).

^¶¶ Supported by the Société Française d'Hématologie, by the Deutsche Forschungsgemeinschaft, and by the Fondation de France.

^|||| Present address and to whom correspondence should be addressed: Département de Biologie Cellulaire, Institut Cochin, INSERM, U567, CNRS, UMR8104, Univ. Paris V, 22 Rue Méchain, F-75014 Paris, France. Tel.: 33-1-40516427; Fax: 33-1-40516430; E-mail: lutz{at}cochin.inserm.fr.

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