Published April 4, 2011 // JCB vol. 193 no. 1 7-16
The Rockefeller University Press, doi: 10.1083/jcb.201010022
© 2011 Ma et al.
Review
Peroxisome assembly: matrix and membrane protein biogenesis
Changle Ma, Gaurav Agrawal, and Suresh Subramani
Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, CA 92093
Correspondence to Suresh Subramani: ssubramani{at}ucsd.edu
C. Ma and G. Agrawal contributed equally to this paper.
Abstract
The biogenesis of peroxisomal matrix and membrane proteins is substantially different from the biogenesis of proteins of other subcellular compartments, such as mitochondria and chloroplasts, that are of endosymbiotic origin. Proteins are targeted to the peroxisome matrix through interactions between specific targeting sequences and receptor proteins, followed by protein translocation across the peroxisomal membrane. Recent advances have shed light on the nature of the peroxisomal translocon in matrix protein import and the molecular mechanisms of receptor recycling. Furthermore, the endoplasmic reticulum has been shown to play an important role in peroxisomal membrane protein biogenesis. Defining the molecular events in peroxisome assembly may enhance our understanding of the etiology of human peroxisome biogenesis disorders.
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