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Mechanism of MEK1 phosphorylation by the N-terminal acidic motif-mediated asymmetric BRAF dimer
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DOI：10.1016/j.molcel.2026.06.039.png)
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Abstract
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• BRAF:MEK1 forms an asymmetric complex mediated by the N-terminal acidic motif • Receiver, but not activator, BRAF protomer forms a canonical active site with a closed P-loop • Phosphorylation of MEK1 Ser222 is captured in the asymmetric complex • The BRAF N-terminal acidic motif is required for full kinase activity
Keywords:
MAPK/ERK signaling
BRAF
MEK
melanoma
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