Peroxisome protein import: a complex journey. (9th June 2016)

• Record Type: Journal Article
• Authors: Baker, Alison; Hogg, Thomas Lanyon; Warriner, Stuart L.
• Is Part Of: Biochemical Society transactions. Volume 44:Number 3(2016)
• Page Start: 783
• Page End: 789
• Publication Date: 2016-06-09
• Subjects: mechanisms -- models -- peroxisome -- PEX5 -- protein import cycle -- targeting signal; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20160036
• Languages: English
• ISSNs: 0300-5127

Abstract

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 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.