Ubiquitination of mammalian pex5p, the peroxisomal import receptor

• Type: Article in International Scientific Journal
• Date: 2007

Authors

carvalho, af (Author) Other; pinto, mp (Author) Other; grou, cp (Author) Other; alencastre, is (Author) Other; fransen, m (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Journal of Biological Chemistry

Vol. 282

Pages: 31267-31272

ISSN: 0021-9258

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 58 Citations

Scopus - 61 Citations

Other information

Authenticus ID: P-004-6QP

DOI: 10.1074/jbc.M70632500

Abstract (EN): Protein translocation across the peroxisomal membrane requires the concerted action of numerous peroxins. One central component of this machinery is Pex5p, the cycling receptor for matrix proteins. Pex5p recognizes newly synthesized proteins in the cytosol and promotes their translocation across the peroxisomal membrane. After this translocation step, Pex5p is recycled back into the cytosol to start a new protein transport cycle. Here, we show that mammalian Pex5p is ubiquitinated at the peroxisomal membrane. Two different types of ubiquitination were detected, one of which is thoil-sensitive, involves Cys(11) of Pex5p, and is necessary for the export of the receptor back into the cytosol. Together with mechanistic data recently described for yeast Pex5p, these findings provide strong evidence for the existence of Pex4p- and Pex22p-like proteins in mammals.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6