TY - JOUR
T1 - Peroxisome homeostasis
T2 - Mechanisms of division and selective degradation of peroxisomes in mammals
AU - Honsho, Masanori
AU - Yamashita, Shun ichi
AU - Fujiki, Yukio
N1 - Funding Information:
We apologize to the colleagues in this field for not citing all their work due to space limitations. We thank K. Shimizu for figure illustrations. This work was supported in part by Grants-in-Aid for Scientific Research ( 24247038 , 25112518 , 25116717 , 26116007 , and 15K14511 to Y.F.; 26440102 to M.H.; 15K18501 to S.Y.) and The Grants for Excellent Graduate Schools from the Ministry of Education, Culture, Sports, Science and Technology of Japan , and grants from Takeda Science Foundation and Japan Foundation for Applied Enzymology .
Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2016/5/1
Y1 - 2016/5/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbamcr.2015.09.032
DO - 10.1016/j.bbamcr.2015.09.032
M3 - Article
C2 - 26434997
AN - SCOPUS:84961124222
VL - 1863
SP - 984
EP - 991
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
SN - 0167-4889
IS - 5
ER -