Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801696 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2016 | 8 Pages |
Abstract
Peroxisome number and quality are maintained by its biogenesis and turnover and are important for the homeostasis of peroxisomes. Peroxisomes are increased in number by division with dynamic morphological changes including elongation, constriction, and fission. In the course of peroxisomal division, peroxisomal morphogenesis is orchestrated by Pex11β, dynamin-like protein 1 (DLP1), and mitochondrial fission factor (Mff). Conversely, peroxisome number is reduced by its degradation. Peroxisomes are mainly degraded by pexophagy, a type of autophagy specific for peroxisomes. Upon pexophagy, an adaptor protein translocates on peroxisomal membrane and connects peroxisomes to autophagic machineries. Molecular mechanisms of pexophagy are well studied in yeast systems where several specific adaptor proteins are identified. Pexophagy in mammals also proceeds in a manner dependent on adaptor proteins. In this review, we address the recent progress in studies on peroxisome morphogenesis and pexophagy. This article is part of a Special Issue entitled: Peroxisomes edited by Ralf Erdmann.
Keywords
MFFubiquitin associatedNbr1DLP1Neighbor of BRCA1 gene 1PexophagyUBAPB1GDAP1Fis1PMPPTSdocosahexaenoic acidChoLIRChinese Hamster Ovaryfission 1DHAperoxisome targeting signalendoplasmic reticulummitochondrial fission factorLC3-interacting regionAIMadaptor proteindynamin-like protein 1peroxisomal membrane proteinCoiled-coilUbiquitin
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Authors
Masanori Honsho, Shun-ichi Yamashita, Yukio Fujiki,