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http://purl.uniprot.org/citations/26972053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26972053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26972053http://www.w3.org/2000/01/rdf-schema#comment"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 binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2016.02.035"xsd:string
http://purl.uniprot.org/citations/26972053http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2016.02.035"xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Gygi S.P."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Gygi S.P."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Sabatini D.M."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Sabatini D.M."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Shen K."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Shen K."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Gygi M.P."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Gygi M.P."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Wyant G.A."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Wyant G.A."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Chantranupong L."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Chantranupong L."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Saxton R.A."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Saxton R.A."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Scaria S.M."xsd:string
http://purl.uniprot.org/citations/26972053http://purl.uniprot.org/core/author"Scaria S.M."xsd:string