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Atg9A trafficking through the recycling endosomes is required for autophagosome formation
- Source :
- Journal of cell science. 129(20)
- Publication Year :
- 2016
-
Abstract
- Autophagy is an intracellular degradation pathway conserved in eukaryote. Among core Autophagy-related (Atg) proteins, mammalian Atg9A is the sole multi-spanning transmembrane protein, and both of the N- and C-terminal domains are exposed to the cytoplasm. It is known that Atg9A travels through the trans-Golgi network (TGN) and the endosomal system under nutrient-rich conditions and transiently localizes to the autophagosome upon autophagy-induction. However, the significance of Atg9A trafficking in autophagosome formation remains elusive. Here we identified sorting motifs at the N-terminal cytosolic stretch of Atg9A, which interact with an adaptor protein, AP-2. Atg9A mutant at the sorting motifs could not execute autophagy and is abnormally accumulated at the recycling endosomes. These combinational defects in autophagy and the Atg9A traffic out of the recycling endosomes were also caused by the knock down of TRAPPC8, a specific subunit of the TRAPPIII complex. These results show directly that the trafficking of Atg9A through the recycling endosomes is an essential step for autophagosome formation.
- Subjects :
- 0301 basic medicine
Autophagosome
Endosome
Protein subunit
Amino Acid Motifs
Adaptor Protein Complex 2
Vesicular Transport Proteins
Autophagy-Related Proteins
Endosomes
Biology
Models, Biological
03 medical and health sciences
symbols.namesake
Structure-Activity Relationship
Salmonella
Autophagy
Animals
Humans
Mice, Knockout
Autophagosomes
Signal transducing adaptor protein
Membrane Proteins
Cell Biology
Golgi apparatus
Transmembrane protein
Endocytosis
Cell biology
Protein Transport
030104 developmental biology
Cytoplasm
Gene Knockdown Techniques
symbols
Tyrosine
HeLa Cells
trans-Golgi Network
Subjects
Details
- ISSN :
- 14779137
- Volume :
- 129
- Issue :
- 20
- Database :
- OpenAIRE
- Journal :
- Journal of cell science
- Accession number :
- edsair.doi.dedup.....4a72e78cb2118efcdfcba715c1b16c0d