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Grou CP Carvalho AF Pinto MP Alencastre IS Rodrigues TA Freitas MO Francisco T Sá-Miranda C Azevedo JE 《Cellular and molecular life sciences : CMLS》2009,66(2):254-262
The peroxisomal protein import machinery displays remarkable properties. Be it its capacity to accept already folded proteins
as substrates, its complex architecture or its energetics, almost every aspect of this machinery seems unique. The list of
unusual properties is still growing as shown by the recent finding that one of its central components, Pex5p, is transiently
monoubiquitinated at a cysteine residue. However, the data gathered in recent years also suggest that the peroxisomal import
machinery is not that exclusive and similarities with p97/Cdc48-mediated processes and with multisubunit RING-E3 ligases are
starting to emerge. Here, we discuss these data trying to distill the principles by which this complex machinery operates.
Received 16 July 2008; received after revision 25 August 2008; accepted 29 August 2008 相似文献
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