The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Two TOR Complexes, Only One of which Is Rapamycin Sensitive, Have Distinct Roles in Cell Growth Control
Open accessAbstract
The target of rapamycin (TOR) proteins in Saccharomyces cerevisiae, TOR1 and TOR2, redundantly regulate growth in a rapamycin-sensitive manner. TOR2 additionally regulates polarization of the actin cytoskeleton in a rapamycin-insensitive manner. We describe two functionally distinct TOR complexes. TOR Complex 1 (TORC1) contains TOR1 or TOR2, KOG1 (YHR186c), and LST8. TORC2 contains TOR2, AVO1 (YOL078w), AVO2 (YMR068w), AVO3 (YER093c), and LST8. FKBP-rapamycin binds TORC1, and TORC1 disruption mimics rapamycin treatment, suggesting that TORC1 mediates the rapamycin-sensitive, TOR-shared pathway. FKBP-rapamycin fails to bind TORC2, and TORC2 disruption causes an actin defect, suggesting that TORC2 mediates the rapamycin-insensitive, TOR2-unique pathway. Thus, the distinct TOR complexes account for the diversity, specificity, and selective rapamycin inhibition of TOR signaling. TORC1 and possibly TORC2 are conserved from yeast to man.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“specifically, mTORC2 contains the mTOR, Rictor, LST8 and SIN1 proteins (Loewith et al., 2002).”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Loewith et al., 2002
In the citing paper
“which was discovered after it was shown that rapamycin is able to inhibit mTORC1 via binding to the protein FKBP12 (REFS31,32).”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [31]
In the citing paper
“mTOR is present in two complexes, mTORC1 (associated with ‘raptor’) and mTORC2 (associated with ‘rictor’), accounting for the diversity, specificity and selectivity of rapamycin-mediated inhibition of TOR signalling”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [31]
Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
Current protocols in molecular biology
Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,281
Sherman, F. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,078
Kim, D., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,051
Bähler, J., Wu, J., Longtine, M. S., Shah, N. G., Mckenzie, A., Steever, A. B., Wach, A., Philippsen, P., & Pringle, J. R. (1998) · Yeast · doi:10.1002/(sici)1097-0061(199807)14:10 · Cited by 2,208
Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast
Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,010
Self-citationTOR, a Central Controller of Cell Growth
Schmelzle, T., & Hall, M. N. (2000) · Cell · doi:10.1016/s0092-8674(00)00117-3 · Cited by 1,914
Self-citationRaptor, a Binding Partner of Target of Rapamycin (TOR), Mediates TOR Action
Hara, K., Maruki, Y., Long, X., Yoshino, K.-I., Oshiro, N., Sujuti, H., Tokunaga, C., Avruch, J., & Yonezawa, K. (2002) · Cell · doi:10.1016/s0092-8674(02)00833-4 · Cited by 1,810
The Tandem Affinity Purification (TAP) Method: A General Procedure of Protein Complex Purification
Puig, Ó., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado‐Nilsson, E., Wilm, M. S., & Séraphin, B. (2001) · Methods · doi:10.1006/meth.2001.1183 · Cited by 1,784
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
Cited by
Sorted by citations
Items 1,001–1,001 of 1,001
Signal integration in the (m)TORC1 growth pathway
Ramlaul, K., & Aylett, C. H. S. (2018) · Frontiers in Biology · doi:10.1007/s11515-018-1501-7 · Cited by 12
Metadata
- Authors
- Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N.
- Affiliations
- University of Basel (CH)
- Corresponding author
- Hall, Michael N.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2002-09
- Volume
- 10
- Issue
- 3
- Pages
- 457-468
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2152600551
- Cited by
- 1,886
- References
- 59
- Citations by year
- 2026: 37 · 2025: 47 · 2024: 68 · 2023: 65 · 2022: 75 · 2021: 79 · 2020: 70 · 2019: 76 · 2018: 76 · 2017: 100 · 2016: 68 · 2015: 115 · 2014: 97 · 2013: 103 · 2012: 135
- FWCI
- 15.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- TOR signaling, TOR1, TOR2, rapamycin sensitivity, cell growth regulation, LST8, Saccharomyces cerevisiae
- MeSH terms
- Actins, Animals, Antifungal Agents, Cell Line, Cytoskeleton, Fungal Proteins, Glycogen, Humans, Protein Binding, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Tissue Distribution, Signal Transduction, Phosphotransferases (Alcohol Group Acceptor), Genes, Reporter, Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Sirolimus, Tacrolimus Binding Proteins, Drug Resistance, Fungal, Saccharomyces cerevisiae Proteins, Macromolecular Substances
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
