Lanyon-Hogg, T, Warriner, SL and Baker, A (2010) Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes. Biology of the Cell, 102 (4). 245 - 263. ISSN 0248-4900
Abstract
Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | peroxisome; protein import; receptor; targeting signal; ubiquitination; targeting signal type-2; rhizomelic chondrodysplasia punctata; arabidopsis leaf peroxisomes; receptor PEX5P interacts; in-vitro import; saccharomyces-cerevisiae; matrix-protein; PTS1 receptor; 3-ketoacyl-coa thiolase; cycling receptor |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 30 Jan 2014 10:27 |
Last Modified: | 15 Sep 2014 02:07 |
Published Version: | http://dx.doi.org/10.1042/BC20090159 |
Status: | Published |
Publisher: | Wiley-Blackwell |
Identification Number: | 10.1042/BC20090159 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:77547 |