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Updated: Mar 14, 2026

Monitoring Stub1-Mediated Pexophagy
Published on: May 12, 2023
Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins
Daniel Effelsberg1, Luis Daniel Cruz-Zaragoza1, Wolfgang Schliebs1
1Abteilung Systembiochemie, Institut für Biochemie und Pathobiochemie, Abteilung Systembiochemie, Ruhr-Universität Bochum, Bochum D-44780, Germany.
Abstract:
Peroxisomal proteins carrying a type 1 peroxisomal targeting signal (PTS1) are recognized by the well-conserved cycling import receptor Pex5p. The yeast YMR018W gene encodes a Pex5p paralog and newly identified peroxin that is involved in peroxisomal import of a subset of matrix proteins. The new peroxin was designated Pex9p, and it interacts with the docking protein Pex14p and a subclass of PTS1-containing peroxisomal matrix enzymes. Unlike Pex5p, Pex9p is not expressed in glucose- or ethanol-grown cells, but it is strongly induced by oleate. Under these conditions, Pex9p acts as a cytosolic and membrane-bound peroxisome import receptor for both malate synthase isoenzymes, Mls1p and Mls2p. The inducible Pex9p-dependent import pathway provides a mechanism for the oleate-inducible peroxisomal targeting of malate synthases. The existence of two distinct PTS1 receptors, in addition to two PTS2-dependent import routes, contributes to the adaptive metabolic capacity of peroxisomes in response to environmental changes and underlines the role of peroxisomes as multi-purpose organelles. The identification of different import routes into peroxisomes contributes to the molecular understanding of how regulated protein targeting can alter the function of organelles according to cellular needs.
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