The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Tti1 and Tel2 Are Critical Factors in Mammalian Target of Rapamycin Complex Assembly
Open accessAbstract
Mammalian target of rapamycin (mTOR) is a member of the phosphatidylinositol 3-kinase-related kinase (PIKK) family and is a major regulator of translation, cell growth, and autophagy. mTOR exists in two distinct complexes, mTORC1 and mTORC2, that differ in their subunit composition. In this study, we identified KIAA0406 as a novel mTOR-interacting protein. Because it has sequence homology with Schizosaccharomyces pombe Tti1, we named it mammalian Tti1. Tti1 constitutively interacts with mTOR in both mTORC1 and mTORC2. Knockdown of Tti1 suppresses phosphorylation of both mTORC1 substrates (S6K1 and 4E-BP1) and an mTORC2 substrate (Akt) and also induces autophagy. S. pombe Tti1 binds to Tel2, a protein whose mammalian homolog was recently reported to regulate the stability of PIKKs. We confirmed that Tti1 binds to Tel2 also in mammalian cells, and Tti1 interacts with and stabilizes all six members of the PIKK family of proteins (mTOR, ATM, ATR, DNA-PKcs, SMG-1, and TRRAP). Furthermore, using immunoprecipitation and size-exclusion chromatography analyses, we found that knockdown of either Tti1 or Tel2 causes disassembly of mTORC1 and mTORC2. These results indicate that Tti1 and Tel2 are important not only for mTOR stability but also for assembly of the mTOR complexes to maintain their activities.
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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Self-citationTOR signaling in growth and metabolism
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Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB
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Self-citationULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
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Cited by
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509
MTOR: a pharmacologic target for autophagy regulation
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The mechanistic target of rapamycin: the grand conducTOR of metabolism and aging
Kennedy, B. K., & Lamming, D. W. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.009 · Cited by 544
Where is mTOR and what is it doing there?
Betz, C., & Hall, M. N. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201306041 · Cited by 527
mTOR complexes in neurodevelopmental and neuropsychiatric disorders
Costa-Mattioli, M., & Monteggia, L. M. (2013) · Nature Neuroscience · doi:10.1038/nn.3546 · Cited by 367
Metadata
- Authors
- Kaizuka, T., Hara, T., Oshiro, N., Kikkawa, U., Yonezawa, K., Takehana, K., Iemura, S.-I., Natsume, T., & Mizushima, N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 285
- Issue
- 26
- Pages
- 20109-20116
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077798795
- Cited by
- 255
- References
- 41
- FWCI
- 5.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kaizuka, T., Hara, T., Oshiro, N., Kikkawa, U., Yonezawa, K., Takehana, K., Iemura, S.-I., Natsume, T., & Mizushima, N. (2010). Tti1 and Tel2 Are Critical Factors in Mammalian Target of Rapamycin Complex Assembly. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m110.121699
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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