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J. Biol. Chem., Vol. 283, Issue 21, 14190-14197, May 23, 2008

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Members of the E2D (UbcH5) Family Mediate the Ubiquitination of the Conserved Cysteine of Pex5p, the Peroxisomal Import Receptor^*

Cláudia P. Grou¹², Andreia F. Carvalho¹², Manuel P. Pinto², Sebastian Wiese^¶, Heike Piechura^¶, Helmut E. Meyer^¶, Bettina Warscheid^¶, Clara Sá-Miranda, and Jorge E. Azevedo³

From the Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal, the Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Largo Professor Abel Salazar, 2, 4009-003 Porto, Portugal, and the ^¶Medizinisches Proteom-Center, Ruhr-Universitaet Bochum, Universitaetsstrasse 150, 44780 Bochum, Germany

According to current models of peroxisomal biogenesis, newly synthesized peroxisomal matrix proteins are transported into the organelle by Pex5p. Pex5p recognizes these proteins in the cytosol, mediates their membrane translocation, and is exported back into the cytosol in an ATP-dependent manner. We have previously shown that export of Pex5p is preceded by (and requires) monoubiquitination of a conserved cysteine residue present at its N terminus. In yeasts, and probably also in plants, ubiquitination of Pex5p is mediated by a specialized ubiquitin-conjugating enzyme, Pex4p. In mammals, the identity of this enzyme has remained unknown for many years. Here, we provide evidence suggesting that E2D1/2/3 (UbcH5a/b/c) are the mammalian functional counterparts of yeast/plant Pex4p. The mechanistic implications of these findings are discussed.

Received for publication, January 16, 2008 , and in revised form, March 7, 2008.

^* This work was supported by grants from Fundação para a Ciência e Tecnologia (PTDC program) and Fundo Europeu de Desenvolvimento Regional, Portugal, by the European Union VI Framework program Grant LSHG-CT-2004-512018, Peroxisomes in Health and Disease, and by a grant from the Deutsche Forschungsgemeinschaft within the SFB 642 and the Land North Rhine-Westphalia, Germany. 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.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental table and a supplemental figure.

¹ Both authors contributed equally to this work.

² Supported by Fundação para a Ciência e Tecnologia.

³ To whom correspondence should be addressed. Tel.: 351-226074900; Fax: 351-226099157; E-mail: jazevedo{at}ibmc.up.pt.

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