Dynamics of membrane-bound G12V KRAS investigated by simulation and single molecule FRET in native nanodiscs

Recent studies have shown that the small GTPase KRAS adopts multiple orientations with respect to the plane of anionic model membranes, whereby either the three C-terminal helices or the three N-terminal ß-strands of the catalytic domain face the membrane. This has functional implications because, in the latter, the membrane occludes the effector-interacting surface. However, it remained unclear how membrane re-orientation occurs and, critically, if it occurs in the cell where KRAS operates as a molecular switch in signaling pathways.

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