期刊
AUTOPHAGY
卷 10, 期 5, 页码 835-845出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/auto.28259
关键词
exportomer; peroxin; peroxisome; pexophagy; Atg36; selective autophagy; Pex1; Pex6
类别
资金
- Wellcome Trust Senior Research Fellowship in Basic Biomedical Science [WT084265MA]
Turnover of damaged, dysfunctional, or excess organelles is critical to cellular homeostasis. We screened mutants disturbed in peroxisomal protein import, and found that a deficiency in the exportomer subunits Pex1, Pex6, and Pex15 results in enhanced turnover of peroxisomal membrane structures compared with other mutants. Strikingly, almost all peroxisomal membranes were associated with phagophore assembly sites in pex1. atg1. cells. Degradation depended on Atg11 and the pexophagy receptor Atg36, which mediates degradation of superfluous peroxisomes. Mutants of PEX1, PEX6, and PEX15 accumulate ubiquitinated receptors at the peroxisomal membrane. This accumulation has been suggested to trigger pexophagy in mammalian cells. We show by genetic analysis that preventing this accumulation does not abolish pexophagy in Saccharomyces cerevisiae. We find Atg36 is modified in pex1. cells even when Atg11 binding is prevented, suggesting Atg36 modification is an early event in the degradation of dysfunctional peroxisomal structures in pex1. cells via pexophagy.
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