Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor

• Type: Article in International Scientific Journal
• Date: 2008

Authors

grou, cp (Author) Other; carvalho, af (Author) Other; pinto, mp (Author) Other; wiese, s (Author) Other; piechura, h (Author) Other; meyer, he (Author) Other; warscheid, b (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Journal of Biological Chemistry

Vol. 283

Pages: 14190-14197

ISSN: 0021-9258

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 52 Citations

Scopus - 54 Citations

Other information

Authenticus ID: P-003-ZBZ

DOI: 10.1074/jbc.M800402200

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8