RRC ID 46063
著者 Lin L, Yang P, Huang X, Zhang H, Lu Q, Zhang H.
タイトル The scaffold protein EPG-7 links cargo-receptor complexes with the autophagic assembly machinery.
ジャーナル J Cell Biol
Abstract The mechanism by which protein aggregates are selectively degraded by autophagy is poorly understood. Previous studies show that a family of Atg8-interacting proteins function as receptors linking specific cargoes to the autophagic machinery. Here we demonstrate that during Caenorhabditis elegans embryogenesis, epg-7 functions as a scaffold protein mediating autophagic degradation of several protein aggregates, including aggregates of the p62 homologue SQST-1, but has little effect on other autophagy-regulated processes. EPG-7 self-oligomerizes and is degraded by autophagy independently of SQST-1. SQST-1 directly interacts with EPG-7 and colocalizes with EPG-7 aggregates in autophagy mutants. Mutations in epg-7 impair association of SQST-1 aggregates with LGG-1/Atg8 puncta. EPG-7 interacts with multiple ATG proteins and colocalizes with ATG-9 puncta in various autophagy mutants. Unlike core autophagy genes, epg-7 is dispensable for starvation-induced autophagic degradation of substrate aggregates. Our results indicate that under physiological conditions a scaffold protein endows cargo specificity and also elevates degradation efficiency by linking the cargo-receptor complex with the autophagic machinery.
巻・号 201(1)
ページ 113-29
公開日 2013-4-1
DOI 10.1083/jcb.201209098
PII jcb.201209098
PMID 23530068
PMC PMC3613692
MeSH Animals Autophagy / physiology* Caenorhabditis elegans / embryology* Caenorhabditis elegans / genetics Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Embryo, Nonmammalian / cytology Embryo, Nonmammalian / embryology* Embryonic Development / physiology* Mutation Protein Multimerization / physiology*
IF 8.811
引用数 45
WOS 分野 CELL BIOLOGY
リソース情報
線虫 tm2508 tm3425