MEK drives BRAF activation through allosteric control of KSR proteins

Hugo Lavoie, Malha Sahmi, Pierre Maisonneuve, Sara A. Marullo, Neroshan Thevakumaran, Ting Jin, Igor Kurinov, Frank Sicheri () and Marc Therrien ()
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Hugo Lavoie: Institute for Research in Immunology and Cancer Laboratory of Intracellular Signaling Université de Montréal C.P. 6128, Succursale Centre-Ville Montréal
Malha Sahmi: Institute for Research in Immunology and Cancer Laboratory of Intracellular Signaling Université de Montréal C.P. 6128, Succursale Centre-Ville Montréal
Pierre Maisonneuve: Lunenfeld-Tanenbaum Research Institute, Sinai Health System
Sara A. Marullo: Institute for Research in Immunology and Cancer Laboratory of Intracellular Signaling Université de Montréal C.P. 6128, Succursale Centre-Ville Montréal
Neroshan Thevakumaran: Lunenfeld-Tanenbaum Research Institute, Sinai Health System
Ting Jin: Institute for Research in Immunology and Cancer Laboratory of Intracellular Signaling Université de Montréal C.P. 6128, Succursale Centre-Ville Montréal
Igor Kurinov: NE-CAT APS, Building 436E, Argonne National Laboratory
Frank Sicheri: Lunenfeld-Tanenbaum Research Institute, Sinai Health System
Marc Therrien: Institute for Research in Immunology and Cancer Laboratory of Intracellular Signaling Université de Montréal C.P. 6128, Succursale Centre-Ville Montréal

Nature, 2018, vol. 554, issue 7693, 549-553

Abstract: KSR–MEK complexes allosterically activate BRAF through the action of N-terminal regulatory region and kinase domain contacts, thus challenging the accepted role of KSR as a scaffold for MEK recruitment to RAF.

Date: 2018
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DOI: 10.1038/nature25478

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