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During this report, we notice that Ser43, Ser259, and Ser621 are the key internet sites of Raf-one which happen to be phosphorylated in mammalian cells and in Sf9 insect cells contaminated that has a recombinant baculovirus encoding human Raf-one. Mutant Raf-1 proteins missing kinase activity also are phosphorylated on these web sites in vivo, indicating that these phosphorylation occasions are usually not a consequence of autophosphorylation. In addition, we notice that Thr268 may be the predominant Raf-one residue phosphorylated in in vitro autokinase assays. Additionally, We now have examined the biochemical exercise of baculovirus-expressed Raf-one proteins made up of mutations at these phosphorylation web sites. In in vitro protein kinase assays Ser259 mutant proteins ended up two-fold extra Lively than wild-style Raf-one and Ser621 mutant proteins were being inactive as kinases.
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