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A Tumor Suppressor Complex with GAP Activity for the Rag GTPases That Signal Amino Acid Sufficiency to mTORC1
Open accessAbstract
Limiting mTORC1: The mTORC1 protein kinase complex has important functions linking metabolism to cell growth and its functions are disrupted in common diseases, including cancer and diabetes. Bar-Peled et al. (p. 1100 ; see the Perspective by Shaw ) discovered regulatory components that help turn down signaling by mTORC1 when cells are deprived of amino acids. Two complexes of proteins, GATOR1 and GATOR2, have opposite effects on activity and cellular localization of mTORC1. Components of the GATOR1 complex negatively regulate mTORC1 and appear to function as tumor supressors. Cancers with loss of GATOR1 function may be particularly amenable to therapeutic strategies that limit activity of mTORC1.
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In the citing paper
“These include CG12090, the Drosophila ortholog of mammalian DEPDC5, which was found to be part of the GATOR1 complex that inhibits the Tor pathway during the protracted course of our studies.”
From Functional unknomics: Systematic screening of conserved genes of unknown function (2023) · cites this paper as [54]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“WDR59 and WDR24 are both subunits of GATOR2 complex, which functions as a positive regulator of amino‐acid‐mediated mTORC1 activation (Bar‐Peled et al., 2013), and WDR24 modulates mTOR through the previously described changes in lysosome cellular positioning and dynamics (Korolchuk et al., 2011) and thus indirectly modulates autophagic flux (Cai et al., 2016).”
From Autophagy gene expression in skeletal muscle of older individuals is associated with physical performance, muscle volume and mitochondrial function in the study of muscle, mobility and aging ( SOMMA ) (2024) · cites this paper as Bar‐Peled et al., 2013
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“Mutants in GATOR1 subunits promote cell growth by increasing Tor activity [54,55].”
From Functional unknomics: Systematic screening of conserved genes of unknown function (2023) · cites this paper as [54]
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“At the Ragulator, the Rag heterodimer interacts with GATOR (GAP Activity Towards Rags), an octomeric complex that controls the activity of the Rag proteins [22].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [22]
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“One of the best described systems for regulating the nucleotide binding status of the Rag GTPases is the activity of the GATOR complexes. GATOR1 functions as a GAP for RagA and RagB, while GATOR2 acts to inhibit the activity of GATOR1 167,168.”
From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [168]
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“One of the best described systems for regulating the nucleotide binding status of the Rag GTPases is the activity of the GATOR complexes. GATOR1 functions as a GAP for RagA and RagB, while GATOR2 acts to inhibit the activity of GATOR1 167,168.”
From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [168]
In the citing paper
“Upstream regulation of the Rag GTPases is more baroque, featuring at least four large protein complexes including: GATOR1, a GAP for RagA/RagB/Gtr1 (Neklesa and Davis, 2009; Bar-Peled et al., 2013; Panchaud et al., 2013a); FLCN-FNIP (Lst4-Lst7 in yeast), a GAP for RagC/RagD/Gtr2 (Péli-Gulli et al., 2015; Petit et al., 2013; Tsun et al., 2013); GATOR2, an inhibitor of GATOR1 (Bar-Peled et al., 2013”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Bar-Peled et al., 2013
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Citations
Cites
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TFEB, Master Regulator of Cellular Clearance
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A TBK1/ULK1 signalling axis couples lysosomal stress to TFEB activation
Esposito, A., Bayramoglu, I., Varriale, C., Cavaliere, M., Brunetti, M. E., Agostinis, R., Jansen, R. M., Tudorica, D. A., Duan, Y.-J., Spacci, M., et al. (2026) · Nature · doi:10.1038/s41586-026-11093-3
“Unlike amino acid starvation, which is known to inhibit RagA/B through the GATOR1 complex 17 , SaliPhe induced TFEB nuclear translocation in both WT and NPRL3 KO cells (Fig.”
Synergistic role of TFEB/TFE3 and mTORC1 in kidney cystogenesis and tumorigenesis
Ferniani, M., Sambri, I., Huynh, T., Pennella, R., Tufano, G., Herz, N. J., Rossi, B., Iannaccone, A., Trepiccione, F., Calcagnì, A., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01881-9
Alves, L. N. R., dos Santos, E. D. V. W., Trabach, R. S. D. R., Meira, D. D., & Louro, I. D. (2026) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2026.131009
mTOR-Mediated Neuron–Cancer Interactions
Nyarkoh, J. K., Wolan, M. J., & Feliciano, D. M. (2026) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases4030024
Tidball, A. M., Luo, J., Walker, J. C., Takla, T. N., Carvill, G. L., & Parent, J. M. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107602 · Cited by 1
Architecture of the human KICSTOR complex and its role in mTORC1 regulation
Yang, A., Li, S., Deng, F., Zuo, P., Wang, W., Dai, Z., Yu, S., Wang, H., Feng, J., Liu, Y., et al. (2026) · Cell Press Blue · doi:10.1016/j.cpblue.2026.100126
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“…crowding defects of lmn-1 mutants by depleting the components of the guanosine triphosphatase– activating protein activity toward Rags (GATOR) complex, specifically the GATOR1 components nprl-2 or nprl-3 , which negatively regulate mTORC1 activity ( 34 ), and quantifying hypodermal GEM diffusion.”
Glycerol 3-phosphate activates lipid metabolism through GATOR2-dependent regulation of mTORC1
Kwon, H., Yamada, S., Meng, L., Kwon, M., Xu, H., Chi, J., Radovick, S., Gu, H., He, L., & Wondisford, F. E. (2026) · Science Signaling · doi:10.1126/scisignal.aeb7989
The Emerging Role of mTOR in Shaping the Cancer Cell Secretome and Plasticity
Cooper, T. T., Topisirović, I., & Postovit, L.-M. M. (2026) · Molecular and Cellular Biology · doi:10.1080/10985549.2026.2699146
Conserved Transcriptomic Signatures of Sirt6 Activity: A Cross-Species RNA-seq Meta-analysisPreprint
Khanna, A., Sharma, R., Xhaferi, S., Kolthur-Seetharam, U., Jiang, P., & Taylor, J. R. (2026) · bioRxiv · doi:10.64898/2026.07.10.735668
“Individual genes with significantly lower expression across Sirt6-low conditions are also related to metabolism, namely Depdc5 , and Abcg2 (Figure 9B and Supplementary Table 22) (Bar-Peled et al., 2013; Takada et al., 2014).”
A genome-wide screen identifies that PLCG2 restrains lysosomal GCase activity
Lawrence, J., Kulkarni, V. V., Tan, C. L., Callow, M. G., Juste, Y., Sangaraju, D., Costa, M., & Bingöl, B. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2514112123
Amino-acids-mTORC1-driven DDA1 phosphorylation promotes DNA repair and glioblastoma progression
Chen, X., Wang, Z., An, Y., Liu, Y., Zhu, R., Li, L., Xu, D., Liu, R., Zhan, X., Yin, B., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03028-2
“…effectors such as S6K1 [17, 18] and 4E-BP1 [19]. mTORC1 activity is tightly regulated on the lysosomal membrane by a host of factors, including Rag GTPases [20, 21], the Ragulator complex [22], GATOR1/2 [23], and amino acid sensors such as Sestrin2 [24, 25], SAMTOR [26], and CASTOR1 [27].”
Circu, M., Castore, R., Latimer, B., Shames, S., Roy, C., Dragoi, A., & Ivanov, S. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1012998
“…– (i) the pentameric Ragulator complex that tethers the Rag GTPase complex to lysosomes [23]; (ii) the GATOR complex (GTPase activating proteins toward Rags), which has GAP activity towards the small RagA/B GTPases [64]; (iii) the Rag GTPase complex, which recruits TORC1 to lysosomes [21,63].”
Li, F., Zhang, S., Duan, H., Wolf, D. A., & Yang, X.-R. (2026) · iScience · doi:10.1016/j.isci.2026.116627
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van der Welle, R. E. N., van der Beek, J., Sanzà, P., Zwartkruis, F. J. T., Liv, N., & Klumperman, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.14.724810
“Phosphorylation of non-canonical substrates by mTORC1 is dependent on the FLCN:FNIP1/2 complex, the GAP required for activation of RagC/D (Bar-Peled et al., 2013; Castellano et al., 2017; Lawrence et al., 2019; Meng & Ferguson, 2018; Petit et al., 2013; Sancak et al., 2010).”
InfluentialInflammation starves antitumour immunity
Denk, D., & Karin, M. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-01933-9
Branch, M., Cha, B., Bartelt, L. C., Shen, W.-C., & Spada, A. L. (2026) · The FASEB Journal · doi:10.1096/fj.202501003r
GATOR1 complex controls cisplatin sensitivity
Pan, Z.-R., Zhang, H.-X., Xiao, X., Brenner, C., & Dokudovskaya, S. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08392-4
Regulation of the Rheb GTPase via GATOR1 ComplexPreprint
Prabhakar, A., & Mair, W. B. (2025) · bioRxiv · doi:10.64898/2025.12.20.695697
“The GATOR1 complex is a validated GAP for RagA/B, and its engagement with RagA has been structurally and Rheb-GATOR1 interaction regulates mTORC1 signaling Prabhakar et al biochemically well established 16,34 .”
InfluentialFBXO2-mediated KPTN ubiquitination promotes amino acid–dependent mTORC1 signaling and tumor growth
Gao, J., Qing, J.-N., Li, X., Luo, Y., Huang, L., Li, H., Zhang, H., Zhang, J., Xiao, P., Li, J., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci195031
“Among these, the GATOR1 complex — comprising DEPDC5, NPRL2, and NPRL3 — acts as a GAP for RagA/B, thereby inhibiting amino acid–stimulated mTORC1 activation (12, 13).”
Hsu, J.-E., Zhao, Q.-Y., Cheng, W.-Q., Kang, H., Brooks, S. V., Kim, M., & Lee, J.-H. (2025) · bioRxiv · doi:10.64898/2025.12.03.692123
“Under amino acid insufficiency, the GATOR1 complex (DEPDC5, NPRL2, and NPRL3) maintains the Rag GTPases (RRAGA/B and RRAGC/D) in their inactive GDP-bound state, thereby preventing mTORC1 from translocating to the lysosomal surface and becoming activated (4,5).”
Nishikubo, K., Ohgaki, R., Okanishi, H., Xu, M.-H., & Kanai, Y. (2025) · Cancer & Metabolism · doi:10.1186/s40170-025-00415-0
“Both amino acids control GATOR1, which negatively regulates mTORC1 kinase activation as a GTPase-activating protein (GAP) for RagA/B GTPases [49–52].”
Yahşi, S., Öksüz, P., Ceviz, K., & Ceylan, C. (2025) · BMC Urology · doi:10.1186/s12894-025-01820-9
“Initially identified as a tumor suppressor gene, NPRL2 has demonstrated such a role in various cancers [13, 14]; however, some in vitro studies have shown that NPRL2 may also act as a tumor promoter in cancer cell lines [15].”
Global conformation of the Rag GTPase heterodimer governs eukaryotic amino acid sensing
Doxsey, D. D., & Shen, K. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2517050122
Song, A., He, Z., Pan, L.-Q., Yu, X., & Li, Y. (2025) · Journal of Food Composition and Analysis · doi:10.1016/j.jfca.2025.108460
Loewith, R., & Tafur, L. (2025) · FEBS Letters · doi:10.1002/1873-3468.70171 · Cited by 2
“In contrast to FLCN-FNIP2, which is a comparably small dimer, the GAP for RagA or RagB forms part of the megadalton-sized, 8-subunit SEA/GATOR complex [55,56].”
Takahashi-Kariyazono, S., Iguchi, A., & Terai, Y. (2025) · BMC Ecology and Evolution · doi:10.1186/s12862-025-02432-5
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Bidirectional Relationship Between Gastroparesis and Malnutrition
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“Amino acid deprivation may specifically be detected by GTPase-activating proteins (or GAPs) which regulate gene recombination, termed the GATOR1 (GAP activity toward recombination-activated genes 1) and GATOR2 (GAP activity toward recombination-activated genes 2) complexes [27].”
DEPDC5-Related Familial Focal Epilepsy With Variable Foci-1: A Report of a Rare Case
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Neuronal cell type specific roles for Nprl2 in neurodevelopmental disorder-relevant behaviors
Dentel, B., Angeles-Perez, L., Flores, A. Y., Lei, K., Ren, C., Sanchez, A. P., & Tsai, P. T. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106790
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“The NPRL3 gene encodes a subunit of the Gap Activity TOward Rags 1 (GATOR1) complex, which negatively regulates the mTOR complex 1 (mTORC1) pathway [14].”
NPRL2 is required for proliferation of oncogenic Ras-transformed bronchial epithelial cells
Chuang, J.-Y., Kuo, H.-H., Wang, P.-H., Su, C.-J., & Yih, L.-H. (2024) · Cell Division · doi:10.1186/s13008-024-00126-w
“…activity toward Rags 1 (GATOR1) complex that inhibits mechanistic target of rapamycin complex 1 (mTORC1) in response to amino acid insufficiency [1]. mTORC1 acts as a serine/ threonine kinase to integrate upstream nutrient and growth factor signals with downstream transcriptional and…”
BackgroundWang, W.-Z., Liang, L., Dai, Z.-L., Zuo, P., Yu, S., Lv, Y., Ding, D., Chen, H.-Y., Jin, Y., Mao, Y., et al. (2023) · bioRxiv · doi:10.1101/2023.10.07.561329
“The human KLHL (1-42) sequences were aligned using Jalview56 and Clustal software57.”
MethodTakahashi-Kariyazono, S., Iguchi, A., & Terai, Y. (2023) · bioRxiv · doi:10.1101/2023.08.03.551769
The Rag GTPases-mTORC1-TFE3 Axis in Kidney Cancer and Neurodevelopment: A Mini Review
Nardone, C., Gu, X., & Elledge, S. J. (2023) · Journal of Neurology & Neuromedicine · doi:10.29245/2572.942x/2023/1.1287
Du, X.-L., Zhao, Z.-P., Zhao, X., Wang, H., Jiang, L., & Tang, W. (2023) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2023.04.063
Seibert, M., Kurrle, N., Stolp, V., Nürnberger, H., Tzschentke, S., Börner, L., Wempe, F., Serve, H., & Schnütgen, F. (2022) · MethodsX · doi:10.1016/j.mex.2022.101929
Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation
Jansen, R. M., Peruzzo, R., Fromm, S. A., Yokom, A. L., Zoncu, R., & Hurley, J. H. (2022) · Science Advances · doi:10.1126/sciadv.add2926 · Cited by 42
“Conversion between active and inactive states is regulated by the RagA/B-specific GAP, GAP activity towards Rags 1 (GATOR1), and by the RagC/D-specific GAP, FLCN:FLCN-interacting protein 2 (FNIP2) ( 16 , 17 ).”
Potts, M. A., Mizutani, S.-Y., Deng, Y., Vaidyanathan, S., Ting, K. E., Giner, G., Sridhar, S., Liao, Y., Diepstraten, S. T., Kueh, A., et al. (2022) · bioRxiv · doi:10.1101/2022.02.16.480657
Royal jelly attenuates metabolic defects in a drosophila mutant with elevated TORC1 activity
Yang, C., Cai, J., Fu, Y., Feng, C., Hao, Y., & Wei, Y. (2020) · Biology Open · doi:10.1242/bio.054999 · Cited by 1
“Nprl3 is a component of GTPase-activating protein towards Rags complex 1 (GATOR1), which inhibits TORC1 activity under nutrient starvation (Bar-Peled et al., 2013; Wei and Lilly, 2014; Wei et al., 2014).”
BackgroundGetting Sucker Punched by Depdc5 Really Hurts
Weston, M. (2020) · Epilepsy Currents · doi:10.1177/1535759720956992
“These papers first identified DEPDC5 as both a frequent cause of familial focal epilepsies(1,2) and a negative regulator of mTOR activity.(3) The discovery of Depdc5’s normal and pathological roles was made more significant by the fact that DEPDC5 was not in the already well-studied canonical PI3K-TSC-mTOR axis, but a…”
BackgroundExostosin-1 Glycosyltransferase Regulates Endoplasmic Reticulum Architecture and DynamicsPreprint
Kerselidou, D., Dohai, B., Nelson, D., Daakour, S., Cock, N. D., Kim, D.-K., Olivet, J., Assal, D. C. E., Jaiswal, A., Saha, D., et al. (2020) · bioRxiv · doi:10.1101/2020.09.02.275925
The Spectrum of DEPDC5 -Related Epilepsy
Salomone, G., Comella, M., Portale, A., Pecora, G., Costanza, G., Bianco, M. L., Sciuto, S., Praticò, E., & Falsaperla, R. (2020) · Journal of Pediatric Neurology online · doi:10.1055/s-0041-1727139
Mathur, P., Santos, C. D. B., Lachuer, H., Latgé, B., Radvanyi, F., Goud, B., & Schauer, K. (2020) · bioRxiv · doi:10.1101/2020.07.10.196931
“Deregulation of mTORC1 signaling and TFEB hyper-activation parallels previous studies in other cancer types (Bar-Peled et al., 2013; Di Malta et al., 2017; Perera and Zoncu, 2016; Perera et al., 2019; Zoncu et al., 2011) and aligns with a genetic study of NMIBC that identified alterations in mTORC1…”
Investigation of mTOR-independent regulation of macroautophagy
Odle, R. I. (2020) · doi:10.17863/cam.51464
Condon, K. J., & Sabatini, D. (2019) · Reactome · doi:10.3180/r-hsa-9639288.2
Self-citation[A second-hit somatic mutation drives neurodevelopmental epilepsy].
Ribierre, T., & Baulac, S. (2019) · Medecine sciences : M/S · doi:10.1051/medsci/2019058
Investigation of Novel Functions of KICSTOR Components in the DNA Damage Response
Pachva, M. C., & Ryan, A. (2018) · Journal of Chemical Environmental and Biological Engineering · doi:10.11648/j.jcebe.20180202.14
“This was then analysed by mass spectrometry and GATOR complex proteins were identified and RNAi (RNA interference) of these newly identified proteins, lead to inhibition of amino acid induced activation of mTORC1 [29].”
BackgroundMethodInfluentialNutrition for Strength Adaptations
Zbinden‐Foncea, H., Avey, A. M., & Baar, K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813922-6.00029-1
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Commentary: GATOR Complex‐Associated Epilepsies
Lemke, J. (2017) · Epilepsia · doi:10.1111/epi.13789
“Together with the natriuretic peptide receptor 2-like proteins NPRL2 and NPRL3, DEPDC5 forms the gap activity towards rags 1 (GATOR1) complex, a repressor of the mechanistic target of rapamycin complex 1 (mTORC1).(5) The link of familial focal epilepsies to the GATOR1 protein complex was followed by the identification…”
BackgroundTemporal and Clonal Progression in a Pediatric Ependymoma Patient Through Multiple TreatmentsPreprint
Miller, C., Dahiya, S., Li, T.-D., Fulton, R., Smyth, M., Dunn, G., Rubin, J., & Mardis, E. (2017) · bioRxiv · doi:10.1101/115923
Cormerais, Y. (2016) · theses.fr (ABES) · doi:10.70675/94cc6971z3a1dz454fzb65dzf153dc0a3a05
“Cependant, ces résultats sont fortement controversés dans la littérature, une autre étude ayant clairement démontré que la protéine LRS ne possède aucune activité GAP (Tsun, Bar-Peled et al. 2013).”
Laboucarié, T. (2016) · theses.fr (ABES) · doi:10.70675/5c52847ez969az4bc3z9144zdedf14c308df
Genetic Counselling in Epilepsy
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The Role of Autophagy and Mitophagy in Liver Diseases
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AMINO ACIDS: SENSING AND IMPLICATION INTO AGING
Lushchak, O. (2015) · Journal of Vasyl Stefanyk Precarpathian National University · doi:10.15330/jpnu.2.1.51-60
“The growth factors regulate kinase activity of mTORC1 and the Rag GTPases recruit mTORC1 to the lysosomal surface to activate it [38].”
BackgroundInfluentialBar-Peled, L. (2014) · Science · doi:10.1126/science.aaa1808
Self-citationA METABOLIC APPROACH FOR THE CONTROL OF GLUTAMINE DEPENDENT TUMORS
Chiu, M. (2014) · doi:10.13130/chiu-martina_phd2014-01-27
“More recently, Sabatini laboratory has identified an octomeric complex, named GATOR, which is a critical regulator of the pathway that signals amino acids sufficiency to mTOR [43].”
Son, S.-M., Li, W.-N., & Rubinsztein, D. (2026) · EXO : beyond the cell · doi:10.70401/exo.2026.0009
“GATOR1, composed of DEP domain containing 5 (DEPDC5), Nitrogen permease regulator 2-like protein (NPRL2), and NPRL3, inactivates mTORC1 by exerting GAP activity toward RagA/B [77–79] .”
Determination of Nutrient Ligand-Sensor Binding Affinity
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GATOR1 gene variants in focal epilepsy
Kovačević, M., Vojvodić, N. M., & Novaković, I. (2024) · Medicinski Podmladak · doi:10.5937/mp75-45140
“…described the role of GTPase-activating protein (GAP) activity towards Rags 1 (GATOR1) complex, consisting of three subunits, DEPDC5, nitrogen permease regulator-like 2 (Nprl2) and nitrogen permease regulator-like 3 (Nprl3) in the mechanistic target of rapamycin (mTOR) molecular pathway (5).”
Deciphering the genetics mechanisms that inhibit synapse formation
Fortes, E. (2020) · doi:10.14288/1.0390272
“The GATOR complex is comprised of two subcomplexes, GATOR1 (containing DEPDC5, Nprl2, and Nprl3), which is inhibited by GATOR2 (Mios, WDR24, WDR59, Seh1L, Sec13) (Bar-peled et al. 2013).”
BackgroundRegulation | mTOR and its Substrates
Proud, C. G., & Xie, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00001-3
Regulation of Telomerase Activity by Rab5 Guanine Nucleotide Exchange Factors
Hambleton, P. (2020) · doi:10.25148/etd.fidc007848
“Loss of the GATOR1 RagGAP results in hyperactive mTORC1 activity that is insensitive to amino acid depletion (Bar-Peled et al., 2013).”
BackgroundSenescence-Associated Beta-Galactosidase Marker of Cellular Senescence
Dimri, M., & Dimri, G. P. (2019) · Reference Module in Biomedical Sciences · doi:10.1016/b978-0-12-801238-3.11446-1
Bisulli, F. (2017) · doi:10.11138/ccre/2017.2.1.037
“Surprisingly, DEPDC5 protein is not connected to the ion-channel function, but its mutations hyper-activate the mammalian target of rapamycin complex 1 (mTORc1), which is an important regulator of cell proliferation, migration and plasticity (9, 10).”
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“acids levels are sufficient, Ragulator’s intrinsic RagA/B GEF activity is stimulated by the v-ATPase, the RagA/B GAP activity of GATOR1 is diminished, and the RagC/D GAP activity of FLCN-FNIP1/2 is activated [123-126].”
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Lamming, D. W. (2015) · Springer eBooks · doi:10.1007/978-3-319-25065-6_3
Upstream regulation of yeast TOR complexes
Stracka, D. (2015) · doi:10.5451/unibas-006450313
“Figure 1: TORC2 signaling Figure 2: TORC1 signaling Figure 3: Nitrogen metabolism core reactions Figure 4: mTORC1 upstream regulation Figure 5: TORC1 upstream regulation Figure 6: TORC1 rapidly phosphorylates Sch9 in response to the nitrogen source Figure 7: The quality of the nitrogen source determines TORC1 activity…”
BackgroundBell, C. (2015) · doi:10.25772/gs4m-z631
“GATOR is composed of GATOR1 and GATOR2, both of which have been found at the lysosome by immunofluorescence, but only GATOR1 interacts directly with the Rags (Bar-Peled et al. 2013; Panchaud, Peli-Gulli, De Virgilio 2013; Schroder et al. 2007).”
Resistance Exercise and Alcohol: Combined Effects on Physiology and Performance
Levitt, D. E. (2018) · University of North Texas Digital Library (University of North Texas) · doi:10.12794/metadc1248374
Metadata
- Authors
- Bar-Peled, L., Chantranupong, L., Cherniack, A. D., Chen, W. W., Ottina, K. A., Grabiner, B. C., Spear, E. D., Carter, S. L., Meyerson, M., & Sabatini, D. M.
- Affiliations
- Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Department of Biology, 9 Cambridge Center, Cambridge, MA 02142, USA.
- Whitehead Institute for Biomedical Research (US)
- Broad Institute (US)
- Johns Hopkins University (US)
- Corresponding author
- Chantranupong, Lynne
- Sabatini, David M.
- ORCID
- Venue
- Science
- Published
- 2013-05-31
- Volume
- 340
- Issue
- 6136
- Pages
- 1100-1106
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3728654
- OpenAlex
- W1519230612
- Cited by
- 1,080
- References
- 32
- Citations by year
- 2026: 40 · 2025: 79 · 2024: 88 · 2023: 89 · 2022: 97 · 2021: 85 · 2020: 91 · 2019: 77 · 2018: 88 · 2017: 83 · 2016: 84 · 2015: 87 · 2014: 69 · 2013: 21
- FWCI
- 38.94
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc)
- PMC
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (CA103866, R01CA103866, R01CA129105, F31CA180271, U24CA143867, P30CA014051)
- National Institute of Allergy and Infectious Diseases (R37AI047389, AI47389), R01AI047389)
- 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 › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- GATOR1, GATOR2, mTORC1, Rag GTPases, GTPase-activating protein, amino acid signaling, lysosomal translocation, DEPDC5, NPRL2, NPRL3, MIO, Sec13, rapamycin sensitivity, amino acid starvation, cancer
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Amino Acids, Carrier Proteins, Humans, Lysosomes, Mutation, Neoplasms, Nuclear Proteins, Proteins, Monomeric GTP-Binding Proteins, GTPase-Activating Proteins, Tumor Suppressor Proteins, RNA, Small Interfering, Cell Line, Tumor, Multiprotein Complexes, HEK293 Cells, TOR Serine-Threonine Kinases
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