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 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.
School of Molecular and Cellular Biology, Astbury Centre for Structural Molecular Biology and Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, U.K. a.baker@leeds.ac.uk.
Alison
A
Baker
Institute of Chemical Biology, Department of Chemistry, Imperial College London, London SW7 2AZ, U.K.
Thomas
T
Lanyon-Hogg
School of Chemistry, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K.
Stuart L
SL
Warriner
D000818:Animals; D056890:Eukaryota / Q000378:metabolism; D006801:Humans; D020675:Peroxisomes / Q000378:metabolism*; D011487:Protein Conformation; D021382:Protein Sorting Signals; D021381:Protein Transport; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*
C529762:PEX5L protein, human; D021382:Protein Sorting Signals; D018160:Receptors, Cytoplasmic and Nuclear
PEX5; mechanisms; models; peroxisome; protein import cycle; targeting signal