{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chantranupong L"],"funding":["NIAID NIH HHS","US NIH","NHGRI NIH HHS","NCI NIH HHS","NIH","John Reed UROP Fund","National Defense Science & Engineering Graduate Fellowship","Department of Defense","NIGMS NIH HHS"],"pagination":["153-164"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4808398"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["165(1)"],"pubmed_abstract":["Amino acids signal to the mTOR complex I (mTORC1) growth pathway through the Rag GTPases. Multiple distinct complexes regulate the Rags, including GATOR1, a GTPase activating protein (GAP), and GATOR2, a positive regulator of unknown molecular function. Arginine stimulation of cells activates mTORC1, but how it is sensed is not well understood. Recently, SLC38A9 was identified as a putative lysosomal arginine sensor required for arginine to activate mTORC1 but how arginine deprivation represses mTORC1 is unknown. Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by "],"journal":["Cell"],"pubmed_title":["The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway."],"pmcid":["PMC4808398"],"funding_grant_id":["R01 GM095567","R01 AI047389","R01CA103866","GM095567","U41 HG006673","R01 CA103866","R37 AI047389","AI47389)","F31 CA189437","F31 CA180271","T32 GM007287","AI47389","P30 CA014051","W81XWH-07-0448"],"pubmed_authors":["Harper JW","Sabatini DM","Chantranupong L","Shen K","Wyant GA","Wang T","Saxton RA","Gygi SP","Scaria SM","Gygi MP"],"additional_accession":[]},"is_claimable":false,"name":"The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway.","description":"Amino acids signal to the mTOR complex I (mTORC1) growth pathway through the Rag GTPases. Multiple distinct complexes regulate the Rags, including GATOR1, a GTPase activating protein (GAP), and GATOR2, a positive regulator of unknown molecular function. Arginine stimulation of cells activates mTORC1, but how it is sensed is not well understood. Recently, SLC38A9 was identified as a putative lysosomal arginine sensor required for arginine to activate mTORC1 but how arginine deprivation represses mTORC1 is unknown. Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Mar","modification":"2025-04-04T00:15:05.571Z","creation":"2019-03-27T03:10:21Z"},"accession":"S-EPMC4808398","cross_references":{"pubmed":["26972053"],"doi":["10.1016/j.cell.2016.02.035"]}}