Through its cyclingbetween a guanosine triphosphate (GTP)-bound “on” stateand a guanosine diphosphate (GDP)-bound “off” state,the protein can respond to extracellular signaling and propagate abiochemical signal via interaction with downstream effectors.1 Activating mutations of KRAS are among the mostcommon driver mutations in human cancers, and frequently alter theprotein’s structure such that GTPase activating proteins (GAPs)are less able to hydrolyze GTP to GDP when bound to KRAS. Here, KRAS is linked to cancer.