mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase - Test2 - elhamkhani - TriplyDB

mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase

mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase

http://www.wikidata.org/entity/Q29616153

about

Guidelines for the use and interpretation of assays for monitoring autophagy Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1 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 SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1 The tumor susceptibility gene TMEM127 is mutated in renal cell carcinomas and modulates endolysosomal function Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1 mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling Glucocerebrosidase is shaking up the synucleinopathies The effects of testosterone deprivation and supplementation on proteasomal and autophagy activity in the skeletal muscle of the male mouse: differential effects on high-androgen responder and low-androgen responder muscle groups Regulation of TOR by small GTPases The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction mTOR signaling in growth control and disease The role of amino acid-induced mammalian target of rapamycin complex 1(mTORC1) signaling in insulin resistance Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases Conserved regulators of Rag GTPases orchestrate amino acid-dependent TORC1 signaling The Emerging Role of Branched-Chain Amino Acids in Insulin Resistance and Metabolism Amino Acid Sensing by mTORC1: Intracellular Transporters Mark the Spot Advances in Autophagy Regulatory Mechanisms The crucial impact of lysosomes in aging and longevity Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance Amino acid management in cancer The neurology of mTOR The molecular basis for load-induced skeletal muscle hypertrophy Autophagy and the (Pro)renin Receptor The role of TRPMLs in endolysosomal trafficking and function mTOR-dependent cell survival mechanisms Regulatory cells and transplantation tolerance Skeletal muscle autophagy: a new metabolic regulator Role of amino acid transporters in amino acid sensing Amino acid sensing in dietary-restriction-mediated longevity: roles of signal-transducing kinases GCN2 and TOR Emerging strategies to effectively target autophagy in cancer Amino acids and mTORC1: from lysosomes to disease Multifaceted role of insulin-like growth factors and mammalian target of rapamycin in skeletal muscle Integration of signals generated by nutrients, hormones, and exercise in skeletal muscle Autophagy modulation as a potential therapeutic target for diverse diseases βA3/A1-crystallin: more than a lens protein Phosphoinositides: tiny lipids with giant impact on cell regulation

P2860

Q21996341-6E1EDA75-2481-4ED7-A860-62BC9FC6163F Q22676705-D481BE8F-7FC1-4835-A7CC-8582E538E573 Q24293153-3ADDD91E-6045-4359-A0BD-014CE618D6B1 Q24294219-B27D5896-3197-4546-87D2-F89E641A5CF5 Q24298767-5797D6F3-2008-49FF-B2A5-02354225CDDE Q24312292-1D0CF85C-4357-4939-A85E-6068BB1DE74C Q24312781-105BA166-9E0A-413B-8CDB-108CBC94B76F Q24313010-59CAC445-598C-4220-854F-5D5882037FA2 Q24315101-CE4E92B7-DF80-4316-9BD6-219BEB2145DB Q24320106-5975AFC4-3922-4ADC-B318-12BCB1A56A77 Q24337392-FF1FAF8A-8A9B-4D13-BFB0-5B78BE393363 Q24596896-0EA8E262-A369-4B4D-9E7A-B1C219E2B5FD Q24598385-22B5ABBE-9397-42FA-9AA4-F42F2028510B Q24603159-F45636FF-3134-40C1-85A9-EE2F021CFEA1 Q24634174-F664D1FC-E6ED-40AA-9E30-AEED66DFAEC5 Q26741046-EF534419-2392-4A38-90FF-1888F1464B4A Q26741088-6108286D-1858-4D5E-B527-DFB4CAD4361F Q26741367-039124D5-5BCE-4BA3-BCBA-230A532CF34E Q26744725-0DB3B5B4-6507-432E-BF23-3D05596B86E5 Q26748629-D6875C2B-A304-48E1-B707-3BD588391DE8 Q26748934-C070FC0A-B471-411D-8E87-5718CF1FD79A Q26749118-2EFFE41A-CDD9-40E0-A6CD-2F9D757B3E22 Q26764871-B11AF50B-8595-4058-B631-20FBA4F39F6B Q26798087-2D4B6F4A-2319-4626-B3DE-DCBCC2A7FD81 Q26824286-A85440C1-9ADA-4E15-B752-6B442BE12A53 Q26829477-759E8A9C-1C8A-4947-8922-2D587D0B1F62 Q26849212-C14150B3-32E2-4915-ABA1-2C6480688F7D Q26864223-72EAEAD0-C307-4603-B548-2ED78DF3304C Q26864688-CD9BC423-06D0-4EEF-B174-5EBF449344E1 Q26865816-42FB7984-51ED-4A5B-B120-867495D7FA7A Q26866957-CE43B6F9-07CA-4CF5-A11B-99C6479FC84C Q26999339-70C133B1-1577-47A8-A333-39EB317F869A Q27001717-FD46D197-F3EB-4EE3-B74E-A4F3C9414853 Q27009194-A9DDD36D-6F6B-4BF6-B5F0-AF3584E1332D Q27009377-995DBE6F-623D-442B-A0AA-A899C4928193 Q27009396-AF1A380B-265A-4DE9-9F5F-34E206BCBC4F Q27009714-F6BD7CD1-2AD9-4E3E-B8A2-537AE61BCA3E Q27010076-BAE41AA1-6950-4925-8572-DF12EFEDA19B Q27012671-E27FE8D2-1212-442C-B3CC-1FB307035B45 Q27012953-AD8B6045-5E44-4F9A-9FBF-9CC327A540D4

P2860

mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase

http://www.wikidata.org/entity/Q29616153

description

2011 nî lūn-bûn

@nan

2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@ast

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@en

type

label

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@ast

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@en

prefLabel

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@ast

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@en

P1433

Q29616153-7B9C9E8A-3461-4EC7-B46B-4125FA530971

P1476

Q29616153-AD660901-BB01-47A9-9D84-38CBF22702A7

P2093

Q29616153-1C450124-5E8A-403B-9D2E-8744E79D9FFC

Q29616153-47689A5F-0CC6-4EBB-89B2-E4E0560CDA6D

Q29616153-D35FCB77-173E-49A9-A352-073271AD6DA0

Q29616153-D56F7C3A-C682-4804-A255-BA6E8FFCD6E5

P2860

Q29616153-1D5E966C-4B24-4A95-95CE-24A5138A493C

Q29616153-332D2677-EF9A-4D64-B198-5BB79DAEFE11

Q29616153-3ACF47DA-7B0B-4C7C-B4A1-B1D81E7DF103

Q29616153-3AD22C65-7819-4812-9D48-DC3A34AA6031

Q29616153-47FDC01B-CC0D-4586-B6F7-0EB5D5F3C081

Q29616153-4880D9AF-5E0A-45AF-AD73-49A2EE6F1FC6

Q29616153-8575250F-EE3F-4A62-84D7-3183D073C89C

Q29616153-87A4AB61-35C7-4C1F-BC5B-B420612B6C4C

Q29616153-8A418106-AD73-4435-895E-3095654EF309

Q29616153-8E87749B-5AE6-4992-8EA7-97078FDB2921

P304

Q29616153-082250ED-BEAF-47C8-8686-815F03AB9417

P31

Q29616153-86181D94-25CE-4360-A086-2B2A3192FF28

P3181

Q29616153-304A3CF0-3B08-4CBA-9B05-4DF7B07E4DC1

P356

Q29616153-22A5FF21-3C44-4120-9897-6BA4F1DA899B

P407

Q29616153-530A832C-5420-475B-953D-59A60A63EBBD

P433

Q29616153-3906D660-0766-4D6C-AC61-F40D4E327972

P478

Q29616153-4C1B10AE-A956-4284-B3AC-66941E8B1530

P50

Q29616153-3760BEB8-FF13-42C9-AA42-524C5125E0DD

Q29616153-C85F823A-4567-4595-980A-946C692722B8

P577

Q29616153-45854F9C-DC6D-469D-A038-BB919168D7C1

P5875

Q29616153-AFDD6811-0643-46F7-8A4F-C6EC553ABEF7

P698

Q29616153-1FCD841F-E5B2-483D-BF9D-7BCDABB5F488

P932

Q29616153-89547F80-3208-454D-9CAE-7889180B026A

P3181

P356

SCIENCE.1207056

P1433

P1476

mTORC1 senses lysosomal amino ...... uires the vacuolar H(+)-ATPase

@en

P2093

Liron Bar-Peled

http://www.w3.org/2001/XMLSchema#string

Roberto Zoncu

http://www.w3.org/2001/XMLSchema#string

Shuyu Wang

http://www.w3.org/2001/XMLSchema#string

Yasemin Sancak

http://www.w3.org/2001/XMLSchema#string

P2860

Requirement of prorenin receptor and vacuolar H+-ATPase-mediated acidification for Wnt signaling

V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway

Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids

The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1

Identification and characterization of a lysosomal transporter for small neutral amino acids

mTOR: from growth signal integration to cancer, diabetes and ageing

Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling

Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb

Regulation of TORC1 by Rag GTPases in nutrient response

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

P304

678-683

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

907787

http://www.w3.org/2001/XMLSchema#string

P356

10.1126/SCIENCE.1207056

http://www.w3.org/2001/XMLSchema#string

P407

P433

6056

http://www.w3.org/2001/XMLSchema#string

P478

334

http://www.w3.org/2001/XMLSchema#string

P50

David M Sabatini

P577

2011-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51769853

http://www.w3.org/2001/XMLSchema#string

P698

22053050

http://www.w3.org/2001/XMLSchema#string

P932

3211112

http://www.w3.org/2001/XMLSchema#string