Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction

Biochemical Journal

Volumn 361, Issue 2, 2002, Pages 255-265

  Liu, Yin ^a   Graham, Caroline ^a   Li, Aiqun ^a   Fisher, Robert J ^a   Shaw, Stephen ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Novel isoform; PKC; T lymphocytes; Turn motif

Indexed keywords

CATALYSIS; HYDROPHOBICITY;

ACTIVATION LOOP;

ENZYME KINETICS;

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN KINASE C; T LYMPHOCYTE RECEPTOR;

ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; MUTANT; PRIORITY JOURNAL; PROTEIN INDUCTION; PROTEIN MOTIF; RECEPTOR UPREGULATION; SIGNAL TRANSDUCTION; T LYMPHOCYTE;

EID: 0037081849     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3610255     Document Type: Article

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