Journal
JOURNAL OF CELL SCIENCE
Volume 129, Issue 20, Pages 3781-3791Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.196196
Keywords
Autophagy; Atg9; Sorting motif; Golgi; Recycling endosome; TRAPP; AP-2
Categories
Funding
- Special Coordination Funds for Promoting Science and Technology of the Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of Japan [25111002, 26111512, 25293372]
- Grants-in-Aid for Scientific Research [25293372, 15H04371, 26111512, 25111002] Funding Source: KAKEN
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Autophagy is an intracellular degradation pathway conserved in eukaryotes. Among core autophagy-related (Atg) proteins, mammalian Atg9A is the sole multi-spanning transmembrane protein, and both of its 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 for autophagosome formation remains elusive. Here, we identified sorting motifs in the N-terminal cytosolic stretch of Atg9A that interact with the adaptor protein AP-2. Atg9A with mutations in the sorting motifs could not execute autophagy and was abnormally accumulated at the recycling endosomes. The combination of defects in autophagy and Atg9A accumulation in the recycling endosomes was also found upon the knockdown 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.
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