About: The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1

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About: The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1 Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2014 (ast) vědecký článek publikovaný v roce 2014 (cs) 2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած (hyw) 2014 թվականի հոտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в жовтні 2014 (uk) wetenschappelijk artikel (gepubliceerd op 2014/10/09) (nl) vedecký článok (publikovaný 2014/10/09) (sk) مقالة علمية (نشرت في 9-10-2014) (ar) article scientifique publié en 2014 (fr) scientific journal article (en) im Oktober 2014 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28118221-41004EA1-5501-46F7-BAF4-E505B20B11EC
publication date	2014-10-09 00:00:00Z (xsd:dateTime)
cites work	wds:Q28118221-04CEBB40-F3AE-47DA-BB12-A1914FB2D348 wds:Q28118221-0C33DCC1-CADE-490C-9314-EB5DDF59F183 wds:Q28118221-12F4028D-85AB-40A2-B0D3-13261E6D999E wds:Q28118221-1C2F1264-8A67-4568-9A4E-B9ED47623227 wds:Q28118221-1E14A479-04AF-4C83-935C-01904AD8E040 wds:Q28118221-242E133B-1C08-434B-A980-C10102428C6F wds:Q28118221-26C5B91F-B8BE-45BF-B0A8-D46A87D4E979 wds:Q28118221-27B394F7-F6DE-4E2A-8EE9-F7F875265AA9 wds:Q28118221-27D9118E-8105-4067-B4C6-99CEFE6894B0 wds:Q28118221-33935212-B573-4F64-B0C9-7A5837C17BF1 wds:Q28118221-3510BA14-81C1-4B30-9CC2-0946189D3F4D wds:Q28118221-390A0993-C976-4F07-86E5-865D3A20CF82 wds:Q28118221-45F6C1BB-2792-4BDC-9B03-884846928F1B wds:Q28118221-465F6A3D-88A2-4631-8CA5-D419A6E5168D wds:Q28118221-4B6CAAB9-8A51-498F-B0EF-D714B8C03A39 wds:Q28118221-512A6455-D411-499B-BEF9-9271534F198D wds:Q28118221-53704D0C-DA45-4F0B-8110-ECDDFCA23C5F wds:Q28118221-54A601B5-EB5C-448C-8A39-4A24882049E8 wds:Q28118221-55532543-A7F9-4A4A-94DF-BF742A3D04FD wds:Q28118221-5F3E9E7D-E5CD-4068-8FFA-EA9954A9773E wds:Q28118221-5FB635CF-C1DD-47DB-AE8C-B43BFFF0EE77 wds:Q28118221-60C23DDE-7C5E-4941-80C2-7E1E298E8A61 wds:Q28118221-65029ED7-A79C-4682-88A5-F959D00E16F3 wds:Q28118221-691BAA56-8272-430D-9930-92E14EA847BF wds:Q28118221-72DC1417-1AA6-45D8-AF49-1BAA5A20C9C7 wds:Q28118221-78654E7D-DE5C-4888-BC7F-85178B814A8C wds:Q28118221-816A15C6-ECC0-44AA-A51A-B60C42D8BB12 wds:Q28118221-85944A3D-E47D-4A30-BFAF-2968CEB8094C wds:Q28118221-88568B67-8BA8-4F26-BEA4-63D7FE891747 wds:Q28118221-8EC69A88-7D2E-4A0F-99F0-2804337FBD90 wds:Q28118221-90B5882D-79F0-47D0-890E-15D47302090B wds:Q28118221-975CB94B-F896-4C06-8E95-BE3F42FD3E93 wds:Q28118221-97A9240E-C50A-4213-A0F2-32D58EACDA81 wds:Q28118221-9B8FC815-C520-4AF3-8FB7-7DC357919051 wds:Q28118221-9C0B57FF-34DF-4697-9A99-E94FCF8231A7 wds:Q28118221-9EF0F0F4-4D87-4F05-A461-DF59B1ABB275 wds:Q28118221-ADC854C8-4DC9-4BD1-A75B-D5E7B1E84153 wds:Q28118221-B424A332-0BEB-4CE4-80C5-2DE090343069 wds:Q28118221-BB9C765D-5F3E-42EE-A948-E8603A451482 wds:Q28118221-C42BFE35-36CB-468F-860D-88E677707F05 wds:Q28118221-D4380FD1-B7D7-45EC-93D0-62F1DDD1B446 wds:Q28118221-D7FA00A6-761B-4259-B442-25C0902EAD78 wds:Q28118221-DAB55302-0D42-4FC7-AB84-2D34D6275083 wds:Q28118221-EF4FDE97-E4D1-4944-BCB6-C41E20233FE3
cites work	The COSMIC (Catalogue of Somatic Mutations in Cancer) database and website Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling mTOR signaling in growth control and disease Insulin activation of Rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2 Rheb binds and regulates the mTOR kinase Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E Rheb promotes cell growth as a component of the insulin/TOR signalling network Rheb is an essential regulator of S6K in controlling cell growth in Drosophila Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex Regulation of mTORC1 by amino acids Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1. Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling Nutrient regulation of the mTOR complex 1 signaling pathway Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival. A growing role for mTOR in promoting anabolic metabolism Regulation of the small GTPase Rheb by amino acids. Novel role of the small GTPase Rheb: its implication in endocytic pathway independent of the activation of mammalian target of rapamycin Nutrient sensing, metabolism, and cell growth control Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1 Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1 Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1 mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase Stressin' Sestrins take an aging fight A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1 Regulation of TORC1 by Rag GTPases in nutrient response Amino acids and mTORC1: from lysosomes to disease Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses Amino acid deprivation inhibits TORC1 through a GTPase-activating protein complex for the Rag family GTPase Gtr1. Localization of Rheb to the endomembrane is critical for its signaling function Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability.

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