Multiple Pathways for Protein Transport to Peroxisomes

Kim, P.K.; Hettema, Ewald H.

doi:10.1016/j.jmb.2015.02.005

Cited by 127 publications

(133 citation statements)

References 188 publications

(271 reference statements)

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“…Analysis of expressed S100A11 was performed in the same way as that in the experiment for which results are shown in Fig. 3d (right) transportation of peroxisomal proteins [32,33]. Among the PEX proteins, only PEX14 bound to S100A11 in a monomeric state (Fig.…”

Section: Effects Of Ca 2+ Binding and Disulfide-bond Formation On S10mentioning

confidence: 97%

Active Secretion of Dimerized S100A11 Induced by the Peroxisome in Mesothelioma Cells

Saho

Satoh

Kondo

et al. 2016

Cancer Microenvironment

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S100A11, a small Ca 2+ binding protein, acts extracellularly as a mediator of cancer progression. That raises the question of how a protein that lacks the classical secretory signal is able to be secreted outside cells without being damaged. Some insights into this question have been obtained, and there has been accumulating evidence indicating a pivotal role of a non-classical vesicle-mediated pathway using lysosomes or peroxisomes for the protein secretion. To obtain a more precise insight into the secretory mechanism of S100A11, we first screened representative cancer cells exhibiting significantly active secretion of S100A11. From the results of profiling, we turned our attention to aggressive cancer mesothelioma cells. In mesothelioma cells, we found that abundant dimeric S100A11 was produced selectively in the peroxisome after transportation of monomeric S100A11 through an interaction with PEX14, a peroxisome membrane protein, resulting in peroxisomal secretion of dimerized S100A11. In an extracellular environment in vitro, dimerized S100A11 promoted mesothelial cell invasion indirectly with the help of fibroblast cells. Overall, the results indicate that the peroxisome functions as an essential vesicle for the production of dimerized S100A11 and the subsequent secretion of the protein from mesothelioma cells and that peroxisome-mediated secretion of dimerized S100A11 might play a critical role in mesothelioma progression in a tumor microenvironment.

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Section: Effects Of Ca 2+ Binding and Disulfide-bond Formation On S10mentioning

confidence: 97%

Active Secretion of Dimerized S100A11 Induced by the Peroxisome in Mesothelioma Cells

Saho

Satoh

Kondo

et al. 2016

Cancer Microenvironment

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“…The diversity and change of enzymatic content is facilitated by conserved and efficient import machinery, enabling directional targeting of folded and oligomerized proteins into the lumen of peroxisomes (reviewed in Kim and Hettema, 2015;Liu et al, 2012;Schliebs et al, 2010). Important determinants of the import cascade are (i) peroxisomal targeting signals (PTSs) exposed by peroxisomal matrix proteins, (ii) cycling import receptors and (iii) multimeric import machinery at the peroxisomal membrane that comprises numerous peroxins (Distel et al, 1996), which import folded proteins.…”

Section: Introductionmentioning

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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“…peroxisome matrix protein import and iii. peroxisome division and proliferation (Schrader et al 2012, Kim andHettema 2015). The import of proteins into the peroxisome matrix depends on two conserved import pathways (for a recent review see Kim and Hettema 2015).…”

Section: Introductionmentioning

confidence: 99%

“…peroxisome division and proliferation (Schrader et al 2012, Kim andHettema 2015). The import of proteins into the peroxisome matrix depends on two conserved import pathways (for a recent review see Kim and Hettema 2015). Each pathway is mediated by a specific import receptor, Pex5 or Pex7, which recognize their targets in the cytosol by means of their peroxisome-targeting sequence PTS1 and PTS2, respectively.…”

Section: Introductionmentioning

confidence: 99%