Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors.
Based on earlier suggestions that peroxisomes may have arisen from endosymbionts that later lost their DNA, it was expected that protein transport into this organelle would have parallels to systems found in other organelles of endosymbiont origin, such as mitochondria and chloroplasts. This review highlights three features of peroxisomal matrix protein import that make it unique in comparison with these other subcellular compartments - the ability of this organelle to transport folded, co-factor-bound and oligomeric proteins, the dynamics of the import receptors during the matrix protein import cycle and the existence of a peroxisomal quality-control pathway, which insures that the peroxisome membrane is cleared of cargo-free receptors.
Léon
Sébastien
S
Section of Molecular Biology, Division of Biological Sciences, University California, Room 3230 Bonner Hall, 9500 Gilman Drive, UC San Diego, La Jolla, CA 92093-0322, USA.
Goodman
Joel M
JM
Subramani
Suresh
S
D003593:Cytoplasm / Q000502:physiology; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008954:Models, Biological; D000074437:Peroxisomal Targeting Signal 2 Receptor; D000074435:Peroxisome-Targeting Signal 1 Receptor; D020675:Peroxisomes / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism; D017510:Protein Folding; D021381:Protein Transport; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism
C116845:PEX18 protein, S cerevisiae; D000074437:Peroxisomal Targeting Signal 2 Receptor; D000074435:Peroxisome-Targeting Signal 1 Receptor; D010940:Plant Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D029701:Saccharomyces cerevisiae Proteins