Baker, A orcid.org/0000-0003-2181-4057, Lanyon Hogg, T and Warriner, SL (2016) Peroxisome protein import: a complex journey. Biochemical Society Transactions, 44 (3). pp. 783-789. ISSN 0300-5127
Abstract
The import of proteins into peroxisomes possesses many unusual features such as the ability to import folded proteins, and a surprising diversity of targeting signals with differing affinities that can be recognised by the same receptor. As understanding of the structure and function of many components of the protein import machinery has grown, an increasingly complex network of factors affecting each step of the import pathway has emerged. Structural studies have revealed the presence of additional interactions between cargo proteins and the PEX5 receptor that affect import potential, with a subtle network of cargo-induced conformational changes in PEX5 being involved in the import process. Biochemical studies have also indicated an interdependence of receptor-cargo import with release of unloaded receptor from the peroxisome. Here we provide an update on recent literature concerning mechanisms of protein import into peroxisomes.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). |
Keywords: | Peroxisome; protein import cycle; mechanisms; models; PEX5; targeting signal |
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) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Jul 2016 15:08 |
Last Modified: | 31 Oct 2016 01:43 |
Published Version: | http://dx.doi.org/10.1042/BST20160036 |
Status: | Published |
Publisher: | Portland Press |
Identification Number: | 10.1042/BST20160036 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:97299 |