Cited by 629Autophagy in Disease and TherapyPI3K/AKT/mTOR signaling in cancerMetabolism, Diabetes, and Cancer

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The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR

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Egan, Dan, Kim, Joungmok, Shaw, Reuben J., Guan, Kun-Liang·2011·Autophagy

DOI 10.4161/auto.7.6.15123PMC PMC3359466

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Abstract

The serine/threonine kinase ULK1 is a mammalian homolog of Atg1, part of the Atg1 kinase complex, which is the most upstream component of the core autophagy machinery conserved from yeast to mammals. In budding yeast, activity of the Atg1 kinase complex is inhibited by TORC1 (target of rapamycin complex 1), but how the counterpart ULK1 complex in mammalian cells is regulated has been unknown. Our laboratories recently discovered that AMPK associates with, and directly phosphorylates, ULK1 on several sites and this modification is required for ULK1 activation after glucose deprivation. In contrast, when nutrients are plentiful, the mTORC1 complex phosphorylates ULK1, preventing its association and activation by AMPK. These studies have revealed a molecular mechanism of ULK1 regulation by nutrient signals via the actions of AMPK and mTORC1.

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AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
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Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
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Additional file 2 of Caprin-1 influences autophagy-induced tumor growth and immune modulation in pancreatic cancer
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Additional file 5 of Cold exposure protects against medial arterial calcification development via autophagy
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Additional file 3 of Cold exposure protects against medial arterial calcification development via autophagy
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Authors: Egan, D., Kim, J., Shaw, R. J., & Guan, K.-L.
Affiliations: Salk Institute for Biological Studies (US)
University of California San Diego (US)
Corresponding author: Shaw, Reuben J.
Guan, Kun-Liang
ORCID: Kim, Joungmok
Shaw, Reuben J.
Guan, Kun-Liang
Venue: Autophagy
Publisher: Informa UK Limited
Published: 2011-06
Volume: 7
Issue: 6
Pages: 643-644
ISSN: 1554-8627 (ISSN-L)
1554-8635
DOI: 10.4161/auto.7.6.15123
PMC: PMC3359466
OpenAlex: W2070871404
Cited by: 627
References: 2
Citations by year: 2026: 20 · 2025: 28 · 2024: 51 · 2023: 33 · 2022: 53 · 2021: 61 · 2020: 57 · 2019: 54 · 2018: 49 · 2017: 56 · 2016: 41 · 2015: 34 · 2014: 42 · 2013: 19 · 2012: 25
FWCI: 21.69
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Autophagy (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01CA108941)
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 › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: ULK1, autophagy initiation, AMPK, mTORC1, protein phosphorylation, nutrient signaling, glucose deprivation, TOR signaling, kinase regulation
MeSH terms: Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Adenylate Kinase, Animals, Autophagy, Saccharomycetales, Glucose, Humans, Models, Biological, Phosphorylation, Proteins, Gene Expression Regulation, Fungal, Caenorhabditis elegans, Protein Serine-Threonine Kinases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Mice, TOR Serine-Threonine Kinases

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The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR

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