PDK1 protein phosphorylation at Thr 354by murine protein serine-threonine kinase 38 contributes to negative regulation of PDK1 protein activity

Journal of Biological Chemistry

Volumn 287, Issue 25, 2012, Pages 20811-20822

  Seong, Hyun A ^a   Jung, Haiyoung ^a,b   Manoharan, Ravi ^a   Ha, Hyunjung ^a  

^a Chungbuk National University   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE-1; APOPTOTIC STIMULI; BIOCHEMICAL MECHANISMS; CELLULAR ENERGY; COMPLEX FORMATIONS; IONOMYCIN; KINASE DOMAINS; KINASE FAMILY; MURINE PROTEINS; NEGATIVE REGULATORS; PLECKSTRIN HOMOLOGY DOMAINS; PROTEIN ACTIVITY; PROTEIN PHOSPHORYLATION; RECEPTOR-ASSOCIATED PROTEINS; THAPSIGARGINS;

AMINO ACIDS; ENZYMES; PHOSPHORYLATION;

PROTEINS;

APOPTOSIS SIGNAL REGULATING KINASE 1; HYDROGEN PEROXIDE; INSULIN; IONOMYCIN; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PLECKSTRIN; PROTEIN 14 3 3; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE KINASE 38; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; THAPSIGARGIN; THREONINE; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NEGATIVE FEEDBACK; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY;

ANIMALS; APOPTOSIS; BASE SEQUENCE; ENZYME ACTIVATION; HEK293 CELLS; HUMANS; HYDROGEN PEROXIDE; MAP KINASE KINASE KINASE 5; MICE; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; OXIDANTS; PHOSPHATIDYLINOSITOL 3-KINASES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; TRANSFORMING GROWTH FACTOR BETA1; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84862294248     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331827     Document Type: Article

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