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Nat Rev Mol Cell Biol. 2010 Dec;11(12):885-90. doi: 10.1038/nrm3008. Epub 2010 Nov 17.

Peroxisomal protein import and ERAD: variations on a common theme.

Author information

1
Ruhr-Universität Bochum, Medizinische Fakultät, Institut für Physiologische Chemie, Abteilung für Systembiochemie, Universitätsstraße 150, D-44780 Bochum, Germany.

Abstract

Despite their distinct biological functions, there is a surprising similarity between the composition of the machinery that imports proteins into peroxisomes and the machinery that degrades endoplasmic reticulum (ER)-associated proteins. The basis of this similarity lies in the fact that both machineries make use of the same basic mechanistic principle: the tagging of a substrate by monoubiquitylation or polyubiquitylation and its subsequent recognition and ATP-dependent removal from a membrane by ATPases of the ATPases associated with diverse cellular activities (AAA) family of proteins. We propose that the ER-associated protein degradation (ERAD)-like removal of the peroxisomal import receptor is mechanically coupled to protein translocation into the organelle, giving rise to a new concept of export-driven import.

PMID:
21081964
DOI:
10.1038/nrm3008
[Indexed for MEDLINE]

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