The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Where is mTOR and what is it doing there?
Open accessAbstract
Target of rapamycin (TOR) forms two conserved, structurally distinct kinase complexes termed TOR complex 1 (TORC1) and TORC2. Each complex phosphorylates a different set of substrates to regulate cell growth. In mammals, mTOR is stimulated by nutrients and growth factors and inhibited by stress to ensure that cells grow only during favorable conditions. Studies in different organisms have reported localization of TOR to several distinct subcellular compartments. Notably, the finding that mTORC1 is localized to the lysosome has significantly enhanced our understanding of mTORC1 regulation. Subcellular localization may be a general principle used by TOR to enact precise spatial and temporal control of cell growth.
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Cites
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
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Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
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Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673
Network organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Termination of autophagy and reformation of lysosomes regulated by mTOR
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Regulation of TORC1 by Rag GTPases in nutrient response
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An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
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Making new contacts: the mTOR network in metabolism and signalling crosstalk
Shimobayashi, M., & Hall, M. N. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3757 · Cited by 1,053
Biochemical and cellular properties of insulin receptor signalling
Haeusler, R. A., McGraw, T. E., & Accili, D. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.89 · Cited by 739
A Method for the Acute and Rapid Degradation of Endogenous Proteins
Clift, D., McEwan, W. A., Labzin, L. I., Konieczny, V., Mogessie, B., James, L. C., & Schuh, M. (2017) · Cell · doi:10.1016/j.cell.2017.10.033 · Cited by 531
mTOR signaling in cellular and organismal energetics
Albert, V., & Hall, M. N. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.001 · Cited by 304
Self-citationAn Ancient, Unified Mechanism for Metformin Growth Inhibition in C. Elegans and Cancer
Wu, L., Zhou, B., Oshiro-Rapley, N., Li, M., Paulo, J. A., Webster, C. M., Mou, F., Kacergis, M. C., Talkowski, M. E., Carr, C. E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.055 · Cited by 227
Metadata
- Authors
- Betz, C., & Hall, M. N.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2013-11-25
- Volume
- 203
- Issue
- 4
- Pages
- 563-574
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2117002197
- Cited by
- 527
- References
- 25
- FWCI
- 18.29
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
