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Atg9A trafficking through the recycling endosomes is required for autophagosome formation

Imai, Kenta, Hao, Feike, Fujita, Naonobu, Tsuji, Yasuhiro, Oe, Yukako, Araki, Yasuhiro, Hamasaki, Maho, Noda, Takeshi, Yoshimori, Tamotsu·2016·Journal of Cell Science
DOI 10.1242/jcs.196196
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Abstract

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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  • In Arabidopsis and some mammalian cells, essentially all ATG5 and ATG12 proteins exist in the conjugated form, and expression levels do not change at least during short-term starvation.

    “In Arabidopsis and some mammalian cells it appears that essentially all of the ATG5 and ATG12 proteins exist in the conjugated form, and the expression levels do not change, at least during short-term starvation [291, 808, 809, 811].”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [811]

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Metadata

Authors
Imai, K., Hao, F., Fujita, N., Tsuji, Y., Oe, Y., Araki, Y., Hamasaki, M., Noda, T., & Yoshimori, T.
Affiliations
  • Graduate School of Frontier Bioscience, Osaka University 1 , 2-2 Yamadaoka, Suita, Osaka 565-0871 , Japan
  • Graduate School of Medicine, Osaka University 2 Department of Genetics , , 2-2 Yamadaoka, Suita, Osaka 565-0871 , Japan
  • Center for Frontier Oral Science, Graduate School of Dentistry, Osaka University 3 , 1-8 Yamadaoka, Suita, Osaka 565-0871 , Japan
ORCID
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2016-10-15
Volume
129
Issue
20
Pages
3781-3791
ISSN
  • 1477-9137
  • 0021-9533
DOI
10.1242/jcs.196196
Cited by
175
References
4
Language
en
Licence
www.biologists.com/user-licence-1-1 (vor, 182 d)
Funders
Ministry of Education, Culture, Sports, Science, and Technology (25111002 26111512 25293372)

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