Pex35 is a regulator of peroxisome abundance

Yofe, Ido; Soliman, Kareem; Chuartzman, Silvia; Morgan, Bruce; Weill, Uri; Yifrach, Eden; Dick, Tobias P.; Cooper, Sara J.; Ejsing, Christer S.; Schuldiner, Maya; Zalckvar, Einat; Thoms, Sven

doi:10.1242/jcs.187914

Cited by 37 publications

(31 citation statements)

References 95 publications

(103 reference statements)

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“…The existence of two distinct PTS1 receptors, Pex5 and Pex9 (in addition to PTS2-dependent import routes), allows yeast cells to adapt the metabolic capacity of peroxisomes to environmental changes. Pex35 was also identified as a new peroxisomal membrane protein in yeast, which is a regulator of peroxisome abundance (Yofe et al 2017 ) whilst the new yeast peroxin, Pex36, a functional homolog of mammalian Pex16, functions in the ER-to-peroxisome traffic of PMPs (Farré et al 2017 ). Finally, a role in the import of matrix proteins required for fatty acid β-oxidation and bile acid synthesis was proposed for the peroxisomal transmembrane protein TMEM135 (PMP52), which has high homology to the TIM17 family that mediates protein translocation across mitochondrial membranes (Renquist et al 2018 ).…”

Section: Mysterious Machinery: New Proteins and Functions At The Peromentioning

confidence: 99%

The peroxisome: an update on mysteries 2.0

Islinger

Voelkl

Fahimi

et al. 2018

Histochem Cell Biol

241

227

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Peroxisomes are key metabolic organelles, which contribute to cellular lipid metabolism, e.g. the β-oxidation of fatty acids and the synthesis of myelin sheath lipids, as well as cellular redox balance. Peroxisomal dysfunction has been linked to severe metabolic disorders in man, but peroxisomes are now also recognized as protective organelles with a wider significance in human health and potential impact on a large number of globally important human diseases such as neurodegeneration, obesity, cancer, and age-related disorders. Therefore, the interest in peroxisomes and their physiological functions has significantly increased in recent years. In this review, we intend to highlight recent discoveries, advancements and trends in peroxisome research, and present an update as well as a continuation of two former review articles addressing the unsolved mysteries of this astonishing organelle. We summarize novel findings on the biological functions of peroxisomes, their biogenesis, formation, membrane dynamics and division, as well as on peroxisome–organelle contacts and cooperation. Furthermore, novel peroxisomal proteins and machineries at the peroxisomal membrane are discussed. Finally, we address recent findings on the role of peroxisomes in the brain, in neurological disorders, and in the development of cancer.

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Section: Mysterious Machinery: New Proteins and Functions At The Peromentioning

confidence: 99%

The peroxisome: an update on mysteries 2.0

Islinger

Voelkl

Fahimi

et al. 2018

Histochem Cell Biol

241

227

View full text Add to dashboard Cite

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“…In S. cerevisiae, Arf1 and Arf3 are ADP-ribosylation factors that upregulate and downregulate peroxisome fission, respectively [93,94]. The double mutant, arf1D pex35D, exhibited an increase in the size and a reduction in the number of peroxisomes, analogous to the phenotype seen in the single mutants arf1D, pex35D, or pex11D cells [92]. The overexpression of Pex35 in arf1D cells restores the normal peroxisome number, suggesting a redundant role between Pex35 and Arf1.…”

Section: Peroxisome Fission In the Growth And Division Modelmentioning

confidence: 99%

Peroxisome biogenesis, membrane contact sites, and quality control

et al. 2018

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Peroxisomes are conserved organelles of eukaryotic cells with important roles in cellular metabolism, human health, redox homeostasis, as well as intracellular metabolite transfer and signaling. We review here the current status of the different co‐existing modes of biogenesis of peroxisomal membrane proteins demonstrating the fascinating adaptability in their targeting and sorting pathways. While earlier studies focused on peroxisomes as autonomous organelles, the necessity of the ER and potentially even mitochondria as sources of peroxisomal membrane proteins and lipids has come to light in recent years. Additionally, the intimate physical juxtaposition of peroxisomes with other organelles has transitioned from being viewed as random encounters to a growing appreciation of the expanding roles of such inter‐organellar membrane contact sites in metabolic and regulatory functions. Peroxisomal quality control mechanisms have also come of age with a variety of mechanisms operating both during biogenesis and in the cellular response to environmental cues.

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“…Peroxisome biogenesis requires peroxins, which are encoded by PEX genes 10 . To date, there are 16 known human peroxins and 35 altogether in all species 7 , 11 . The majority of peroxins are integral peroxisomal membrane proteins (PMPs).…”

Section: Introductionmentioning

confidence: 99%

Super-resolution imaging reveals the sub-diffraction phenotype of Zellweger Syndrome ghosts and wild-type peroxisomes

Soliman

Göttfert

Rosewich

et al. 2018

Sci Rep

Self Cite

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Peroxisomes are ubiquitous cell organelles involved in many metabolic and signaling functions. Their assembly requires peroxins, encoded by PEX genes. Mutations in PEX genes are the cause of Zellweger Syndrome spectrum (ZSS), a heterogeneous group of peroxisomal biogenesis disorders (PBD). The size and morphological features of peroxisomes are below the diffraction limit of light, which makes them attractive for super-resolution imaging. We applied Stimulated Emission Depletion (STED) microscopy to study the morphology of human peroxisomes and peroxisomal protein localization in human controls and ZSS patients. We defined the peroxisome morphology in healthy skin fibroblasts and the sub-diffraction phenotype of residual peroxisomal structures (‘ghosts’) in ZSS patients that revealed a relation between mutation severity and clinical phenotype. Further, we investigated the 70 kDa peroxisomal membrane protein (PMP70) abundance in relationship to the ZSS sub-diffraction phenotype. This work improves the morphological definition of peroxisomes. It expands current knowledge about peroxisome biogenesis and ZSS pathoethiology to the sub-diffraction phenotype including key peroxins and the characteristics of ghost peroxisomes.

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Pex35 is a regulator of peroxisome abundance

Cited by 37 publications

References 95 publications

The peroxisome: an update on mysteries 2.0

The peroxisome: an update on mysteries 2.0

Peroxisome biogenesis, membrane contact sites, and quality control

Super-resolution imaging reveals the sub-diffraction phenotype of Zellweger Syndrome ghosts and wild-type peroxisomes

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