期刊
AUTOPHAGY
卷 14, 期 3, 页码 368-384出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2017.1413521
关键词
Atg30; Atg37; autophagic receptor; peroxin; peroxisome; Pex3; pexophagy; receptor-protein complex; selective autophagy
类别
资金
- HHS \ NIH \ National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) [DK41737]
- UC San Diego Frontiers of Innovation Scholars Program (FISP) [P0034]
- European Molecular Biology Organization (EMBO) [EMBO ALTF 1238-2014]
- HHS \ NIH \ National Institute of General Medical Sciences (NIGMS) [GM119571]
Macroautophagy/autophagy is a highly conserved process in which subcellular components destined for degradation are sequestered within autophagosomes. The selectivity of autophagy is determined by autophagy receptors, such as Pichia pastoris Atg30 (autophagy-related 30), which controls the selective degradation of peroxisomes (pexophagy) through the assembly of a receptor-protein complex (RPC). Previously, we proved that the peroxisomal acyl-CoA-binding protein, Atg37, and the highly conserved peroxin, Pex3, are required for RPC formation and efficient pexophagy. Here, we describe how Atg37 and Pex3 regulate the assembly and activation of the pexophagic RPC. We demonstrate that Atg30 requires both Atg37 and Pex3 to recruit Atg8 and Atg11 to the pexophagic RPC, because Atg37 depends on Pex3 for its localization at the peroxisomal membrane. We establish that due to close proximity of Atg37- and Pex3-binding sites in the middle domain of Atg30, the binding of these proteins to Atg30 is mutually exclusive within this region. We also show that direct binding of Pex3 and Atg37 to Atg30 regulates its phosphorylation by the Hrr25 kinase, negatively and positively, respectively. Based on these results we present a model that clarifies the assembly and activation of the pexophagic RPC through the phosphoregulation of Atg30.
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