c-Cbl tyrosine kinase-binding domain mutant G306E abolishes the interaction of c-Cbl with CD38 and fails to promote retinoic acid-induced cell differentiation and G0 arrest

Journal of Biological Chemistry

Volumn 284, Issue 38, 2009, Pages 25664-25677

  Shen, Miaoqing ^a   Yen, Andrew ^a,b  

^a Cornell University ^*  (United States)

^b VRT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; CELL DIFFERENTIATION; HL-60 CELLS; IMMUNOPRECIPITATES; LEUKEMIA CELLS; MAPK SIGNALING; MYELOID DIFFERENTIATION; NB4 CELLS; RETINOIC ACIDS; RING FINGER; SIGNALING COMPLEX; TRANSFECTANTS; TYROSINE KINASE; WILD TYPES;

ACIDS; AMINO ACIDS; CELL MEMBRANES; DRIVES;

SIGNALING;

CBL PROTEIN; CD38 ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE; MUTANT PROTEIN; PROTEIN TYROSINE KINASE; RETINOIC ACID; RING FINGER PROTEIN; SYNAPTOPHYSIN; ANTINEOPLASTIC AGENT; CBL PROTEIN, HUMAN; CD38 PROTEIN, HUMAN; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; MULTIPROTEIN COMPLEX; PHOSPHOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SLP 76 SIGNAL TRANSDUCING ADAPTOR PROTEINS; SLP-76 SIGNAL TRANSDUCING ADAPTOR PROTEINS; VAV PROTEIN;

ARTICLE; CELL CYCLE ARREST; CELL CYCLE G0 PHASE; CELL DIFFERENTIATION; CONTROLLED STUDY; GENETIC ASSOCIATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; WILD TYPE; AMINO ACID SUBSTITUTION; BIOLOGICAL MODEL; CELL STRAIN HL 60; DRUG EFFECT; GENETICS; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SUBSTITUTION; ANTIGENS, CD38; ANTINEOPLASTIC AGENTS; CELL DIFFERENTIATION; G0 PHASE; HL-60 CELLS; HUMANS; MAP KINASE SIGNALING SYSTEM; MEMBRANE GLYCOPROTEINS; MODELS, BIOLOGICAL; MULTIPROTEIN COMPLEXES; MUTATION, MISSENSE; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHOPROTEINS; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-CBL; PROTO-ONCOGENE PROTEINS C-VAV; TRETINOIN;

EID: 70350004020     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.014241     Document Type: Article

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