Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy.
By N. Hosokawa, Taichi Hara, T. Kaizuka, C. Kishi, A. Takamura, Yutaka Miura, S. Iemura, Tohru Natsume, K. Takehana, Naoyuki Yamada and 3 more. Molecular Biology of the Cell, 2009
1,988 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/4ff77b05524f0c81e67b8f4b37c654cbd54d981f
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In Epidemiology
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- Guido Kroemer
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- D. Klionsky
- Alec C. Kimmelman
- Douglas R. Green
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In Molecular Biology
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- David M. Sabatini
- Beth Levine
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- M. Laplante
- Alec C. Kimmelman
In Physiology
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Citations in the corpus
- mTOR signaling at a glance (2009, background): “Activation of S6K1 by mTORC1 promotes the phosphorylation of IRS1 and reduces its stability (reviewed by Harrington et al., 2005 ).”
- ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. (2009, background): “Hosokawa et al. (2009) showed that mTOR interacts with the ULK1-Atg13-FIP200 complex in a nutrientdependent manner and phosphorylates ULK1 and Atg13.”
- mTOR signaling in growth control and disease (2012, positive): “In mammals, mTORC1 directly phosphorylates and suppresses ULK1/Atg13/FIP200 (unc-51-like kinase 1/mammalian autophagy-related gene 13/focal adhesion kinase family-interacting protein of 200 kDa), a kinase complex required to initiate autophagy (Figure 2B) (Ganley et al., 2009; Hosokawa et al., 2009;”
- AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1 (2011, background): “Accumulating reports have suggested that there is also a relationship between Ulk1 and mTORC1 in mammalian cell”