Cited by 2,076Autophagy in Disease and TherapyPI3K/AKT/mTOR signaling in cancerCalcium signaling and nucleotide metabolism

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Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

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Hosokawa, Nao, Hara, Taichi, Kaizuka, Takeshi, Kishi, Chieko, Takamura, Akito, Miura, Yutaka, Iemura, Shun-ichiro, Natsume, Tohru, Takehana, Kenji, Yamada, Naoyuki, Guan, Jun-Lin, Oshiro, Noriko, Mizushima, Noboru·2009·Molecular Biology of the Cell

DOI 10.1091/mbc.e08-12-1248PMC PMC2663915

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Abstract

Autophagy is an intracellular degradation system, by which cytoplasmic contents are degraded in lysosomes. Autophagy is dynamically induced by nutrient depletion to provide necessary amino acids within cells, thus helping them adapt to starvation. Although it has been suggested that mTOR is a major negative regulator of autophagy, how it controls autophagy has not yet been determined. Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable ∼3-MDa protein complex with ULK1 and FIP200. Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. In contrast to yeast counterparts, formation of the ULK1–Atg13–FIP200 complex is not altered by nutrient conditions. Importantly, mTORC1 is incorporated into the ULK1–Atg13–FIP200 complex through ULK1 in a nutrient-dependent manner and mTOR phosphorylates ULK1 and Atg13. ULK1 is dephosphorylated by rapamycin treatment or starvation. These data suggest that mTORC1 suppresses autophagy through direct regulation of the ∼3-MDa ULK1–Atg13–FIP200 complex.

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Authors: Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., Guan, J.-L., Oshiro, N., & Mizushima, N.
Affiliations: Tokyo Medical and Dental University (JP)
National Institute of Advanced Industrial Science and Technology (JP)
Exploratory Research, Pharmaceutical Research Laboratory, and
Ajinomoto (Japan) (JP)
University of Michigan (US)
Biosignal Research Center, Kobe University (JP)
ORCID: Hara, Taichi
Kaizuka, Takeshi
Miura, Yutaka
Natsume, Tohru
Guan, Jun-Lin
Mizushima, Noboru
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2009-04
Volume: 20
Issue: 7
Pages: 1981-1991
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.e08-12-1248
PMC: PMC2663915
OpenAlex: W2156144699
Cited by: 2,076
References: 54
Citations by year: 2026: 68 · 2025: 81 · 2024: 133 · 2023: 128 · 2022: 139 · 2021: 171 · 2020: 154 · 2019: 132 · 2018: 114 · 2017: 128 · 2016: 132 · 2015: 142 · 2014: 115 · 2013: 112 · 2012: 110
FWCI: 73.07
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Molecular Biology of the Cell (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: University of Tokyo
Tokyo Medical and Dental University
Toray Science Foundation
Japan Society for the Promotion of Science
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: autophagy, mTORC1, ULK1, ATG13, FIP200, autophagosome formation, nutrient signaling, mTOR phosphorylation, rapamycin, starvation, lysosomal degradation
MeSH terms: Autophagy-Related Proteins, Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Autophagy, Cell Line, Cell Membrane, Humans, Molecular Weight, Phosphorylation, Protein Binding, Protein Kinases, Proteins, Transcription Factors, Protein Serine-Threonine Kinases, Protein Transport, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, TOR Serine-Threonine Kinases

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Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

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