Final answer:
The false statement would likely pertain to the RTK's ability to catalyze the autophosphorylation reaction; kinase activity could enable this process. Disruption in transmembrane dimerization or RAS GTPase activity can have varied effects on signaling duration and cell behavior, potentially leading to cancer.
Therefore, Option C is correct.
Step-by-step explanation:
The statement most likely to be false regarding a situation where a receptor tyrosine kinase (RTK) was transversely moved in the membrane but retained its kinase activity is that it wouldn't be able to catalyze the autophosphorylation reaction even if the ligand could bind. If the kinase activity is intact, then autophosphorylation could still occur since the ATP binding site should be functional. However, the ability of the RTK to propagate its signaling message downstream or find its ligand intracellularly could be compromised.
Regarding EGFR signaling, a mutation in the transmembrane region that affects dimerization could lead to either an active signal for a longer or shorter duration, or lack of signaling, depending on whether the receptor can still dimerize and subsequently activate the signaling pathway. In the case where GTPase activity of RAS is inhibited, RAS protein activation would persist, leading to continuous signaling and, potentially, to uncontrolled cell growth (e.g., cancer).