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 |