Cellular and Molecular Life Sciences

, Volume 66, Issue 2, pp 254–262

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

  • C. P. Grou
  • A. F. Carvalho
  • M. P. Pinto
  • I. S. Alencastre
  • T. A. Rodrigues
  • M. O. Freitas
  • T. Francisco
  • C. Sá-Miranda
  • J. E. Azevedo
Review

DOI: 10.1007/s00018-008-8415-5

Cite this article as:
Grou, C.P., Carvalho, A.F., Pinto, M.P. et al. Cell. Mol. Life Sci. (2009) 66: 254. doi:10.1007/s00018-008-8415-5

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.

Pex5ptransient ubiquitinationperoxisomal biogenesisnatively unfolded domainprotein translocation

Copyright information

© Birkhäuser Verlag, Basel 2008

Authors and Affiliations

  • 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
  1. 1.Instituto de Biologia Molecular e Celular (IBMC)Universidade do PortoPortoPortugal
  2. 2.Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)Universidade do PortoPortoPortugal
  3. 3.Faculdade de CiênciasUniversidade do PortoPortoPortugal