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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2008 Sep 22;66(2):254–262. doi: 10.1007/s00018-008-8415-5

The peroxisomal protein import machinery – a case report of transient ubiquitination with a new flavor

C P Grou 1,2, A F Carvalho 1,2, M P Pinto 1,2, I S Alencastre 1,2, T A Rodrigues 1,2,3, M O Freitas 1,2, T Francisco 1, C Sá-Miranda 1, J E Azevedo 1,2,
PMCID: PMC11131494  PMID: 18810320

Abstract.

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.

Keywords. Pex5p, transient ubiquitination, peroxisomal biogenesis, natively unfolded domain, protein translocation

Footnotes

Received 16 July 2008; received after revision 25 August 2008; accepted 29 August 2008


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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