The peroxisomal protein import machinery - a case report of transient ubiquitination with a new flavor

• Type: Another Publication in an International Scientific Journal
• Date: 2009

Authors

grou, cp (Author) Other; carvalho, af (Author) Other; pinto, mp (Author) Other; alencastre, is (Author) Other; rodrigues, ta (Author) Other; freitas, mo (Author) Other; francisco, t (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Cellular and Molecular Life Sciences

Vol. 66

Pages: 254-262

ISSN: 1420-682X

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 25 Citations

Scopus - 28 Citations

Other information

Authenticus ID: P-003-PBS

DOI: 10.1007/s00018-008-8415-5

Abstract (EN): The peroxisomal protein import machinery displays remarkable properties. Be it its capacity to accept already folded proteins as substrates, its complex architecture or its energetics, almost every aspect of this machinery seems unique. The list of unusual properties is still growing as shown by the recent finding that one of its central components, Pex5p, is transiently monoubiquitinated at a cysteine residue. However, the data gathered in recent years also suggest that the peroxisomal import machinery is not that exclusive and similarities with p97/Cdc48-mediated processes and with multisubunit RING-E3 ligases are starting to emerge. Here, we discuss these data trying to distill the principles by which this complex machinery operates.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9