Import of proteins into the peroxisomal matrix

Hasan, Sharizal; Platta, Harald W.; Erdmann, Ralf

doi:10.3389/fphys.2013.00261

Cited by 74 publications

(64 citation statements)

References 135 publications

(177 reference statements)

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“…Pex5p recognizes its cargo proteins in the cytosol, and the receptor-cargo complex docks at the peroxisomal membrane through interaction with either Pex14p or Pex13p (Hasan et al, 2013). Subsequently, Pex5p together with Pex14p forms a transient import pore, which allows traversal of folded proteins across the membrane (Meinecke et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Effelsberg

Cruz-Zaragoza

Schliebs

et al. 2016

Journal of Cell Science

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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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Section: Discussionmentioning

confidence: 99%

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Effelsberg

Cruz-Zaragoza

Schliebs

et al. 2016

Journal of Cell Science

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“…The maintenance of peroxisomes depends on the formation of the peroxisomal membrane and the subsequent import of both membrane and matrix proteins (1,2). All peroxisomal matrix proteins are nuclearly encoded, synthesized on free ribosomes, and imported posttranslationally into the organelle (3).…”

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“…The authors declare that they have no conflicts of interest with the contents of this article. 1 To whom correspondence should be addressed: Institute of Biochemistry and Pathobiochemistry, Ruhr-University Bochum, Universitätsstr. 150, D-44780 Bochum, Germany.…”

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Structural Insights into Cargo Recognition by the Yeast PTS1 Receptor

Hagen

Drepper

Fischer

et al. 2015

Journal of Biological Chemistry

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Background: Peroxisomal proteins are recognized in the cytosol by the import receptor Pex5p. Results: Photo-cross-linking and mass spectrometry reveal the binding interface of Pex5p and its cargo protein Pcs60p. Conclusion: Pex5p-cargo interaction extends beyond signal sequence recognition and exhibits a bivalent binding mode. Significance: These data indicate a two-step concept of peroxisomal cargo recognition with initial tethering and subsequent lock-in.

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“…The pathway followed by PEX5 during the protein transport process is reasonably known (25)(26)(27)(28). After binding a cargo protein in the cytosol, PEX5 interacts with the peroxisomal docking/ translocation machinery (DTM) (29), a peroxisomal membrane protein complex comprising PEX13, PEX14, and the RING peroxins PEX2, PEX10, and PEX12 (30)(31)(32).…”

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A PEX7-Centered Perspective on the Peroxisomal Targeting Signal Type 2-Mediated Protein Import Pathway

Rodrigues

Alencastre

Francisco

et al. 2014

Molecular and Cellular Biology

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dPeroxisomal matrix proteins are synthesized on cytosolic ribosomes and transported to the organelle by shuttling receptors. Matrix proteins containing a type 1 signal are carried to the peroxisome by PEX5, whereas those harboring a type 2 signal are transported by a PEX5-PEX7 complex. The pathway followed by PEX5 during the protein transport cycle has been characterized in detail. In contrast, not much is known regarding PEX7. In this work, we show that PEX7 is targeted to the peroxisome in a PEX5-and cargo-dependent manner, where it becomes resistant to exogenously added proteases. Entry of PEX7 and its cargo into the peroxisome occurs upstream of the first cytosolic ATP-dependent step of the PEX5-mediated import pathway, i.e., before monoubiquitination of PEX5. PEX7 passing through the peroxisome becomes partially, if not completely, exposed to the peroxisome matrix milieu, suggesting that cargo release occurs at the trans side of the peroxisomal membrane. Finally, we found that export of peroxisomal PEX7 back into the cytosol requires export of PEX5 but, strikingly, the two export events are not strictly coupled, indicating that the two proteins leave the peroxisome separately. P eroxisomal matrix proteins are synthesized on cytosolic ribosomes and posttranslationally targeted to the organelle via one of two peroxisomal targeting sequences (PTSs): (i) the PTS type 1 (PTS1), a small peptide frequently ending with the sequence SKL located at the C terminus of the vast majority of matrix proteins (1, 2), and (ii) the PTS2, a degenerated nonapeptide present at the amino terminus of a few matrix proteins (3-5). In contrast to the PTS1, the PTS2 is generally cleaved when the protein reaches the organelle matrix (5-7). In mammals and many other organisms, both PTS1 and PTS2 proteins are transported to the organelle by PEX5, the peroxisomal shuttling receptor (8-11). The interaction of PEX5 with PTS1 proteins is direct (12-16), whereas the interaction between PEX5 and PTS2 proteins requires the adaptor protein PEX7 (17-19). Interestingly, not all PEX5 proteins in a mammalian cell are capable of binding PEX7. This is due to alternative splicing of the PEX5 transcript, which yields two major isoforms of the receptor, PEX5S and PEX5L. In contrast to PEX5L, PEX5S is not able to bind PEX7 because it lacks an internal 37-amino-acid domain (8, 10). The situation in yeasts is different. While these organisms also use PEX5 to target PTS1 proteins to the peroxisome, import of PTS2 proteins is promoted by PEX7 and a species-specific member of the so-called PEX20 family (19-23), a group of proteins that have no mammalian counterpart but that display functional similarities with the N-terminal half of PEX5L (17,19,24).The pathway followed by PEX5 during the protein transport process is reasonably known (25-28). After binding a cargo protein in the cytosol, PEX5 interacts with the peroxisomal docking/ translocation machinery (DTM) (29), a peroxisomal membrane protein complex comprising PEX13, PEX14, and the RING peroxins PEX2, PE...

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Import of proteins into the peroxisomal matrix

Cited by 74 publications

References 135 publications

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Structural Insights into Cargo Recognition by the Yeast PTS1 Receptor

A PEX7-Centered Perspective on the Peroxisomal Targeting Signal Type 2-Mediated Protein Import Pathway

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