Receptor recognition by the peroxisomal AAA-complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p.

The receptor-cycle of type I peroxisomal matrix protein import is completed by ubiquitination of the membrane-bound receptor Pex5p and its subsequent export back to the cytosol. The receptor export is the only ATP-dependent step of the whole process and is facilitated by two members of the AAA family of proteins ...
(ATPases associated with various cellular activities), namely Pex1p and Pex6p. To gain further insight into substrate recognition by the AAA complex, we generated an N-terminally linked ubiquitin-Pex5p fusion protein. This fusion protein displayed biological activity as it is able to functionally complement a PEX5-deletion in S. cerevisiae. In vitro assays revealed its interaction at wild-type level with the native cargo protein Pcs60p and Pex14p, constituent of the receptor docking-complex. We also demonstrate in vitro deubiquitination by the deubiquitinating enzyme Ubp15p. In vitro pull-down assays and crosslinking studies demonstrate that Pex5p recognition by the AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p.
J. Biol. Chem.
Date: Aug. 10, 2018
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