title: Peroxisome homeostasis: Mechanisms of division and selective degradation of peroxisomes in mammals.
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.
authors.affiliation: Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.
authors.forename: Masanori
authors.initials: M
authors.lastname: Honsho
authors.affiliation: Department of Cellular Physiology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata 951-8510, Japan.
authors.forename: Shun-ichi
authors.initials: S
authors.lastname: Yamashita
authors.affiliation: Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan. Electronic address: yfujiki@kyudai.jp.
authors.forename: Yukio
authors.initials: Y
authors.lastname: Fujiki
mesh_terms: D000818:Animals; D034281:Dynamins; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000074401:Peroxins; D020675:Peroxisomes / Q000737:chemistry / Q000378:metabolism*; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D059748:Proteolysis; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D013045:Species Specificity; D025801:Ubiquitin / Q000235:genetics / Q000378:metabolism*; D015003:Yeasts / Q000737:chemistry / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D024101:Mitochondrial Proteins; C092128:PEX11 protein, S cerevisiae; D000074401:Peroxins; D020033:Protein Isoforms; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D020558:GTP Phosphohydrolases; C110768:DNM1L protein, human; D034281:Dynamins
keywords: Adaptor protein; Growth and division; Peroxisomal division; Peroxisomal morphogenesis; Peroxisome turnover; Pexophagy