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- W1739822153 abstract "In a yeast two-hybrid screen we identified a member of the 14-3-3 family of proteins that can bind to Bcr. 14-3-3 beta binds to the serine/threonine rich region B in the kinase domain encoded by the first exon. In this paper we show by co-immunoprecipitation that Bcr binds to Raf in vivo and we argue that this interaction is mediated by 14-3-3 dimers, based on the following findings. First, 14-3-3 isoforms bind to both Raf and Bcr. Second, Bcr does not bind to Raf directly in the two-hybrid system, but co-expression of 14-3-3 beta allows complex formation. Third, Bcr, 14-3-3 proteins and Raf co-elute in gel filtration and in sequential ion exchange chromatography and the three proteins can be co-immunoprecipitated from the the separate fractions, indicating that they are present in a ternary complex. Moreover, approximately 10 times more Raf is bound to Bcr, and vice versa, in the membrane fraction (where Raf is activated) than in the cytosolic fraction. We suggest a new function for 14-3-3 proteins as a novel type of new function for 14-3-3 proteins as a novel type of adaptor which acts by dimerization and binding to different proteins." @default.
- W1739822153 created "2016-06-24" @default.
- W1739822153 creator A5076863478 @default.
- W1739822153 creator A5082685256 @default.
- W1739822153 date "1995-10-01" @default.
- W1739822153 modified "2023-10-15" @default.
- W1739822153 title "Bcr and Raf form a complex in vivo via 14-3-3 proteins." @default.
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- W1739822153 doi "https://doi.org/10.1002/j.1460-2075.1995.tb00165.x" @default.
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