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过氧化物酶体稳态:哺乳动物中过氧化物酶体的分裂和选择性降解机制

Peroxisome homeostasis: Mechanisms of division and selective degradation of peroxisomes in mammals.

作者信息

Honsho Masanori, Yamashita Shun-ichi, Fujiki Yukio

机构信息

Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.

Department of Cellular Physiology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata 951-8510, Japan.

出版信息

Biochim Biophys Acta. 2016 May;1863(5):984-91. doi: 10.1016/j.bbamcr.2015.09.032. Epub 2015 Oct 3.

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.

摘要

过氧化物酶体的数量和质量通过其生物发生和周转得以维持,这对于过氧化物酶体的稳态至关重要。过氧化物酶体通过分裂增加数量,伴随动态形态变化,包括伸长、缢缩和裂变。在过氧化物酶体分裂过程中,过氧化物酶体形态发生由Pex11β、动力蛋白样蛋白1(DLP1)和线粒体裂变因子(Mff)协调。相反,过氧化物酶体数量通过其降解而减少。过氧化物酶体主要通过pexophagy(一种对过氧化物酶体特异的自噬类型)降解。在pexophagy过程中,一种衔接蛋白定位于过氧化物酶体膜上,并将过氧化物酶体与自噬机制相连。在酵母系统中对pexophagy的分子机制进行了深入研究,其中鉴定出了几种特定的衔接蛋白。哺乳动物中的pexophagy也以依赖衔接蛋白的方式进行。在本综述中,我们阐述了过氧化物酶体形态发生和pexophagy研究的最新进展。

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