Abstract
Despite their distinct biological functions, there is a surprising similarity between the composition of the machinery that imports proteins into peroxisomes and the machinery that degrades endoplasmic reticulum (ER)-associated proteins. The basis of this similarity lies in the fact that both machineries make use of the same basic mechanistic principle: the tagging of a substrate by monoubiquitylation or polyubiquitylation and its subsequent recognition and ATP-dependent removal from a membrane by ATPases of the ATPases associated with diverse cellular activities (AAA) family of proteins. We propose that the ER-associated protein degradation (ERAD)-like removal of the peroxisomal import receptor is mechanically coupled to protein translocation into the organelle, giving rise to a new concept of export-driven import.
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Change history
17 November 2010
We have updated the link to Ralf Erdmann's homepage in the online version of this article.
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Acknowledgements
We are grateful to S. Wüthrich for technical assistance. This work was supported by the Deutsche Forschungsgemeinschaft, Germany (SFB642).
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Schliebs, W., Girzalsky, W. & Erdmann, R. Peroxisomal protein import and ERAD: variations on a common theme. Nat Rev Mol Cell Biol 11, 885–890 (2010). https://doi.org/10.1038/nrm3008
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DOI: https://doi.org/10.1038/nrm3008
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