Regulation of peroxisome dynamics by phosphorylation
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- 作者：Silke Oeljeklausa ; 1 ; Andreas Schummera ; 1 ; Thomas Mastalskib ; Harald W. Plattab ; Bettina Warscheida ; c ; bettina.warscheid@biologie.uni-freiburg.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：CK ; casein kinase ; Cvt ; cytoplasm-to-vacuole targeting ; DRPs ; dynamin-related proteins ; ER ; endoplasmic reticulum ; EPCONS ; ER-to-peroxisome contact sites ; mPTS ; membrane peroxisomal targeting signal ; MS ; mass spectrometry ; mTOR ; mammalian target of rapamycin ; PAS ; pre-autophagosomal structure ; PMP ; peroxisomal membrane protein ; PTM ; posttranslational modification ; PTS ; peroxisomal targeting signal ; SGD ; Saccharomyces Genome Database ; TOM ; translocase of the outer mitochondrial membrane ; TSC ; tub
- 刊名：Biochimica et Biophysica Acta (BBA)-Molecular Cell Research
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1863
- 期：5
- 页码：1027-1037
- 全文大小：967 K
文摘
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Proteins involved in peroxisome biogenesis and degradation are phosphorylated in vivo.
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Phosphorylation of Pex11p regulates its activity and binding to Fis1p.
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Inp2p involved in peroxisome inheritance is phosphorylated in a cell cycle-dependent manner.
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The serine/threonine kinase Hrr25p phosphorylates pexophagy receptors.
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The removal of peroxisomes by pexophagy is controlled by the phosphorylation of the autophagy receptors Atg30p and Atg36p.