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

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

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  • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Abstract Text:

    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.

    The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Publishing Authors By Initials

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

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Science (New York, N.Y.)

    VOLUME: 320

    Page Numbers: 1496-501

    Journal Abbreviation: Science

    ISSN: 1095-9203

    DAY: 22

    MONTH: 05

    YEAR: 2008

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

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    LANGUAGE: eng

    NlmUniqueID: 404511

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    Grant and Affiliation Information for The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1.

    AFFILIATION: Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology (MIT), Nine Cambridge Center, Cambridge, MA 02142, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCI

    GRANT: R01 CA103866

    ACRONYM: CA

    MEDLINETA: Science

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