Blog
About

80
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

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

      Science (New York, N.Y.)

      Adaptor Proteins, Signal Transducing, Amino Acids, metabolism, Cell Line, Cell Nucleus, Cytoplasm, Dimerization, Guanosine Triphosphate, Humans, Insulin, Leucine, Monomeric GTP-Binding Proteins, genetics, Multiprotein Complexes, Mutant Proteins, Mutation, Neuropeptides, Phosphorylation, Protein Binding, Protein Kinases, Proteins, Signal Transduction, TOR Serine-Threonine Kinases, Transcription Factors

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The multiprotein mTORC1 protein kinase complex is the central component of a pathway that promotes growth in response to insulin, energy levels, and amino acids and is deregulated in common cancers. We find that the Rag proteins--a family of four related small guanosine triphosphatases (GTPases)--interact with mTORC1 in an amino acid-sensitive manner and are necessary for the activation of the mTORC1 pathway by amino acids. A Rag mutant that is constitutively bound to guanosine triphosphate interacted strongly with mTORC1, and its expression within cells made the mTORC1 pathway resistant to amino acid deprivation. Conversely, expression of a guanosine diphosphate-bound Rag mutant prevented stimulation of mTORC1 by amino acids. The Rag proteins do not directly stimulate the kinase activity of mTORC1, but, like amino acids, promote the intracellular localization of mTOR to a compartment that also contains its activator Rheb.

          Related collections

          Author and article information

          Journal
          18497260
          2475333
          10.1126/science.1157535

          Comments

          Comment on this article