Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C

Science

Volumn 280, Issue 5360, 1998, Pages 109-112

  Marais, Richard ^a   Light, Yvonne ^a   Mason, Clive ^a   Paterson, Hugh ^a   Olson, Michael F ^a   Marshall, Christopher J ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; RAF PROTEIN; RAS PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME SUBSTRATE; MONKEY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

ANIMALS; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CERCOPITHECUS AETHIOPS; COS CELLS; ENZYME ACTIVATION; ENZYME INHIBITORS; EPIDERMAL GROWTH FACTOR; GUANOSINE TRIPHOSPHATE; INDOLES; MUTATION; PROTEIN KINASE C; PROTO-ONCOGENE PROTEINS C-RAF; RAS PROTEINS; RECEPTORS, MUSCARINIC; SIGNAL TRANSDUCTION; TETRADECANOYLPHORBOL ACETATE;

ANIMALIA;

EID: 0032478610     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5360.109     Document Type: Article

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46. 2, but only 0.05% v/v 2-mercaptoethanol (medium-salt buffer). DNA was sheared, and extracts were clarified by centrifugation (13,000g for 2 min); protein concentrations were measured with a Bio-Rad protein assay kit. Immunoblots for endogenous Ras or Raf-1 were done with monoclonal antibodies (products no. 02120 and no. R19120, Transduction Laboratories). For Ras-Raf complex analysis by immunoblot, endogenous Ras or Raf-1 was immunoprecipitated from ≃15 mg of cellular protein with either 10 μg of Y13-238 or 10 μg of Raf-1 monoclonal antibody and probed by immunoblotting for Raf-1 or Ras. For assay of Ras-associated GSTMek-1 activation, Ras was immunoprecipitated from ∼3.5 mg of cellular protein with Y13-238 (10 μg), washed four times with low-salt buffer, and assayed as described (17, 24). Ras immunoprecipitates were eluted with extraction buffer (40 μl), diluted with dilution buffer (160 μl) (17), and reprecipitated with Raf-1 monoclonal antibody (2 μg). Measurements of Ras-GTP were done as described (23). The cells were extracted in medium-salt buffer, and proteins (∼3 mg) were absorbed to bacterially expressed GSTRBD. Ras proteins were revealed by immunoblotting. In control experiments using GSTR89LRBD, Ras-GTP was not detected (73).