Letter abstract


Nature Cell Biology 7, 817 - 822 (2005)
Published online: 10 July 2004 | doi:10.1038/ncb1281

Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol

Harald W. Platta1,2, Silke Grunau1,2, Katja Rosenkranz1, Wolfgang Girzalsky1 & Ralf Erdmann1

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Peroxisomal import receptors bind their cargo proteins in the cytosol and target them to docking and translocation machinery at the peroxisomal membrane (reviewed in ref. 1). The receptors release the cargo proteins into the peroxisomal lumen and, according to the model of cycling receptors, they are supposed to shuttle back to the cytosol. This shuttling of the receptors has been assigned to peroxins including the AAA peroxins Pex1p and Pex6p, as well as the ubiquitin-conjugating enzyme Pex4p (reviewed in ref. 2). One possible target for Pex4p is the PTS1 receptor Pex5p, which has recently been shown to be ubiquitinated3, 4, 5. Pex1p and Pex6p are both cytosolic and membrane-associated AAA ATPases of the peroxisomal protein import machinery, the exact function of which is still unknown. Here we demonstrate that the AAA peroxins mediate the ATP-dependent dislocation of the peroxisomal targeting signal-1 (PTS1) receptor from the peroxisomal membrane to the cytosol.

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  1. Institut für Physiologische Chemie, Abt. Systembiochemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany.
  2. These authors contributed equally to this work.

Correspondence to: Ralf Erdmann1 Ralf.Erdmann@rub.de



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