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Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex

Sarbassov, Dos D ; Guertin, David A ; Ali, Siraj M ; Sabatini, David M

Science (American Association for the Advancement of Science), 2005-02, Vol.307 (5712), p.1098-1101 [Periódico revisado por pares]

Washington, DC: American Association for the Advancement of Science

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Título:
Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex
Autor: Sarbassov, Dos D ; Guertin, David A ; Ali, Siraj M ; Sabatini, David M
Assuntos: 3-Phosphoinositide-Dependent Protein Kinases ; Adaptor Proteins, Signal Transducing ; Animals ; B lymphocytes ; Biochemistry ; Biological and medical sciences ; Birds of prey ; Cancer ; Cancer genetics ; Carrier Proteins - metabolism ; Cell Line ; Cell Line, Tumor ; Cell lines ; Cellular biology ; Double stranded RNA ; Drosophila ; Drosophila melanogaster ; Drosophila Proteins - metabolism ; Enzyme Activation ; Enzymes ; Gene expression regulation ; General aspects ; Genetic aspects ; HeLa cells ; HT29 cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunoprecipitation ; Inhibition ; Literary Devices ; Medical sciences ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphorylation ; Protein kinases ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases - metabolism ; Proteins - metabolism ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-akt ; Rapamycin ; Rapamycin-Insensitive Companion of mTOR Protein ; Regulatory-Associated Protein of mTOR ; RNA Interference ; Serine - metabolism ; TOR Serine-Threonine Kinases ; Tumors
É parte de: Science (American Association for the Advancement of Science), 2005-02, Vol.307 (5712), p.1098-1101
Notas: ObjectType-Article-1
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Descrição: Deregulation of Akt/protein kinase B (PKB) is implicated in the pathogenesis of cancer and diabetes. Akt/PKB activation requires the phosphorylation of Thr³⁰⁸ in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser⁴⁷³ within the carboxyl-terminal hydrophobic motif by an unknown kinase. We show that in Drosophila and human cells the target of rapamycin (TOR) kinase and its associated protein rictor are necessary for Ser⁴⁷³ phosphorylation and that a reduction in rictor or mammalian TOR (mTOR) expression inhibited an Akt/PKB effector. The rictor-mTOR complex directly phosphorylated Akt/PKB on Ser⁴⁷³ in vitro and facilitated Thr³⁰⁸ phosphorylation by PDK1. Rictor-mTOR may serve as a drug target in tumors that have lost the expression of PTEN, a tumor suppressor that opposes Akt/PKB activation.
Editor: Washington, DC: American Association for the Advancement of Science
Idioma: Inglês

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Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex

Sarbassov, Dos D ; Guertin, David A ; Ali, Siraj M ; Sabatini, David M

Washington, DC: American Association for the Advancement of Science

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