| Literature DB >> 28783719 |
Zhan Yao1, Rona Yaeger2, Vanessa S Rodrik-Outmezguine1, Anthony Tao3, Neilawattie M Torres1, Matthew T Chang4,5,6, Matthias Drosten7, Huiyong Zhao1, Fabiola Cecchi8, Todd Hembrough8, Judith Michels9,10, Hervé Baumert11, Linde Miles1,12, Naomi M Campbell13, Elisa de Stanchina1, David B Solit2,4,14, Mariano Barbacid7, Barry S Taylor4,5,14, Neal Rosen1,2,15.
Abstract
Approximately 200 BRAF mutant alleles have been identified in human tumours. Activating BRAF mutants cause feedback inhibition of GTP-bound RAS, are RAS-independent and signal either as active monomers (class 1) or constitutively active dimers (class 2). Here we characterize a third class of BRAF mutants-those that have impaired kinase activity or are kinase-dead. These mutants are sensitive to ERK-mediated feedback and their activation of signalling is RAS-dependent. The mutants bind more tightly than wild-type BRAF to RAS-GTP, and their binding to and activation of wild-type CRAF is enhanced, leading to increased ERK signalling. The model suggests that dysregulation of signalling by these mutants in tumours requires coexistent mechanisms for maintaining RAS activation despite ERK-dependent feedback. Consistent with this hypothesis, melanomas with these class 3 BRAF mutations also harbour RAS mutations or NF1 deletions. By contrast, in lung and colorectal cancers with class 3 BRAF mutants, RAS is typically activated by receptor tyrosine kinase signalling. These tumours are sensitive to the inhibition of RAS activation by inhibitors of receptor tyrosine kinases. We have thus defined three distinct functional classes of BRAF mutants in human tumours. The mutants activate ERK signalling by different mechanisms that dictate their sensitivity to therapeutic inhibitors of the pathway.Entities:
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Year: 2017 PMID: 28783719 PMCID: PMC5648058 DOI: 10.1038/nature23291
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962