Journal
BIOCHEMICAL JOURNAL
Volume 451, Issue -, Pages 345-352Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20130078
Keywords
biogenesis; endoplasmic reticulum; peroxin; peroxisome; peroxisome membrane protein; quality control
Categories
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Boehringer Ingelheim Fonds
- BBSRC [BB/E013740/1, BBS/E/C/00005207, BB/F007108/1, BB/F007299/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E013740/1, BB/F007299/1, BBS/E/C/00005207, BB/F007108/1] Funding Source: researchfish
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PMPs (peroxisome membrane proteins) play essential roles in organelle biogenesis and in co-ordinating peroxisomal metabolism with pathways in other subcellular compartments through transport of metabolites and the operation of redox shuttles. Although the import of soluble proteins into the peroxisome matrix has been well studied, much less is known about the trafficking of PMPs. Pex3 and Pex19 (and Pex16 in mammals) were identified over a decade ago as critical components of PMP import; however, it has proved surprisingly difficult to produce a unified model for their function in PMP import and peroxisome biogenesis. It has become apparent that each of these peroxins has multiple functions and in the present review we focus on both the classical and the more recently identified roles of Pex19 and Pex3 as informed by structural, biochemical and live cell imaging studies. We consider the different models proposed for peroxisome biogenesis and the role of PMP import within them, and propose that the differences may be more perceived than real and may reflect the highly dynamic nature of peroxisomes.
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