Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Science

Volumn 307, Issue 5712, 2005, Pages 1098-1101

  Sarbassov, Dos D ^a   Guertin, David A ^a   Ali, Siraj M ^a   Sabatini, David M ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; COMPLEXATION; DRUG PRODUCTS; PATHOLOGY; TUMORS;

HUMAN CELLS; PATHOGENESIS; PHOSPHORYLATION; PROTEIN KINASE B (PKB);

ENZYMES;

CELL PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOINOSITIDE DEPENDENT KINASE 1; PROTEIN KINASE B; RICTOR PROTEIN; SERINE; TARGET OF RAPAMYCIN KINASE; THREONINE; UNCLASSIFIED DRUG;

MEDICINE;

ANIMAL CELL; ARTICLE; CANCER; CANCER INHIBITION; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; DIABETES MELLITUS; DROSOPHILA; DRUG TARGETING; EFFECTOR CELL; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; IN VITRO STUDY; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ANIMALS; CARRIER PROTEINS; CELL LINE; CELL LINE, TUMOR; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; ENZYME ACTIVATION; HUMANS; HYDROPHOBICITY; IMMUNOPRECIPITATION; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN-SERINE-THREONINE KINASES; PROTEINS; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-AKT; RNA INTERFERENCE; SERINE;

ANIMALIA; ARACHNIDA; HEXAPODA; MAMMALIA;

EID: 13844312400     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1106148     Document Type: Article

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31. This work was supported by a grant from the NIH (R01 AI47389) and awards from the Pew Charitable Trust and the Rita Allen Foundation to D.M.S., as well as fellowships from the Anna Fuller Fund to D.D.S., Damon Runyon Cancer Research Foundation to D.A.G., and the Howard Hughes Medical Institute to S.M.A. We thank members of the Sabatini lab for suggestions on the manuscript and M. B. Yaffe for helpful discussions. Molecular interaction data have been deposited in the Biomolecular Interaction Network Database with accession codes 19S918 to 19S923.