| Literature DB >> 27678487 |
Daniel Effelsberg1, Luis Daniel Cruz-Zaragoza1, Wolfgang Schliebs1, Ralf Erdmann2.
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.Entities:
Keywords: Malate synthases; Mls1p; Mls2p; PTS1; Peroxisomal targeting signal; Peroxisome; Pex5p receptor; Pex9p; Protein import
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Year: 2016 PMID: 27678487 DOI: 10.1242/jcs.195271
Source DB: PubMed Journal: J Cell Sci ISSN: 0021-9533 Impact factor: 5.285