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Molecular and Cellular Biology, December 2001, p. 8035-8044, Vol. 21, No. 23
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.23.8035-8044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of Components of the Murine Histone Deacetylase 6 Complex: Link between Acetylation and Ubiquitination Signaling Pathways

Daphné Seigneurin-Berny,1 André Verdel,1 Sandrine Curtet,1 Claudie Lemercier,1 Jérôme Garin,2 Sophie Rousseaux,1 and Saadi Khochbin1,*

Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Equipe Chromatine et Expression des Gènes, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex,1 and Laboratoire de Chimie des Protéines, CEA, Grenoble,2 France

Received 13 June 2001/Accepted 27 August 2001

The immunopurification of the endogenous cytoplasmic murine histone deacetylase 6 (mHDAC6), a member of the class II HDACs, from mouse testis cytosolic extracts allowed the identification of two associated proteins. Both were mammalian homologues of yeast proteins known to interact with each other and involved in the ubiquitin signaling pathway: p97/VCP/Cdc48p, a homologue of yeast Cdc48p, and phospholipase A2-activating protein, a homologue of yeast UFD3 (ubiquitin fusion degradation protein 3). Moreover, in the C-terminal region of mHDAC6, a conserved zinc finger-containing domain named ZnF-UBP, also present in several ubiquitin-specific proteases, was discovered and was shown to mediate the specific binding of ubiquitin by mHDAC6. By using a ubiquitin pull-down approach, nine major ubiquitin-binding proteins were identified in mouse testis cytosolic extracts, and mHDAC6 was found to be one of them. All of these findings strongly suggest that mHDAC6 could be involved in the control of protein ubiquitination. The investigation of biochemical properties of the mHDAC6 complex in vitro further supported this hypothesis and clearly established a link between protein acetylation and protein ubiquitination.

* Corresponding author. Mailing address: Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Equipe Chromatine et Expression des Gènes, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex, France. Fax: (33) 4 76 54 95 95. Phone: (33) 4 76 54 95 83. E-mail: khochbin{at}ujf-grenoble.fr.

Molecular and Cellular Biology, December 2001, p. 8035-8044, Vol. 21, No. 23
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.23.8035-8044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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