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Peroxisome protein import: a complex journey

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 recognized by the same receptor. As understanding of the structure and function of many compone...

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Detalles Bibliográficos
Autores principales: Baker, Alison, Hogg, Thomas Lanyon, Warriner, Stuart L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4900764/
https://www.ncbi.nlm.nih.gov/pubmed/27284042
http://dx.doi.org/10.1042/BST20160036
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author Baker, Alison
Hogg, Thomas Lanyon
Warriner, Stuart L.
author_facet Baker, Alison
Hogg, Thomas Lanyon
Warriner, Stuart L.
author_sort Baker, Alison
collection PubMed
description 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 recognized 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.
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spelling pubmed-49007642016-06-23 Peroxisome protein import: a complex journey Baker, Alison Hogg, Thomas Lanyon Warriner, Stuart L. Biochem Soc Trans Biochemical Society Focused Meetings 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 recognized 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. Portland Press Ltd. 2016-06-09 2016-06-15 /pmc/articles/PMC4900764/ /pubmed/27284042 http://dx.doi.org/10.1042/BST20160036 Text en © 2016 The Author(s) http://creativecommons.org/licenses/by/4.0/ 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) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Biochemical Society Focused Meetings
Baker, Alison
Hogg, Thomas Lanyon
Warriner, Stuart L.
Peroxisome protein import: a complex journey
title Peroxisome protein import: a complex journey
title_full Peroxisome protein import: a complex journey
title_fullStr Peroxisome protein import: a complex journey
title_full_unstemmed Peroxisome protein import: a complex journey
title_short Peroxisome protein import: a complex journey
title_sort peroxisome protein import: a complex journey
topic Biochemical Society Focused Meetings
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4900764/
https://www.ncbi.nlm.nih.gov/pubmed/27284042
http://dx.doi.org/10.1042/BST20160036
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