Question
What would be the effect on a G protein's activity if:a. its GAP were inhibited?b. its guanine nucleotide exchange protein were inhibited?
Step 1
G proteins are molecular switches that toggle between an active state (when bound to GTP) and an inactive state (when bound to GDP). Their activity is regulated by two main types of proteins: GTPase-activating proteins (GAPs) and guanine nucleotide exchange Show more…
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1. If Ran GAPs are mutated such they are non-functional, A) Ran will remain active until its native GTPase activity hydrolyzes GTP B) Ran will be more rapidly inactivated C) both of the above 2. If Ran GEFs are mutated such they are no longer functional, A) Ran will be rapidly activated B) When Ran attains its GDP-bound state, it will remain in that form C) Ran will more rapidly bind GTP
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Signal-transducing trimeric G proteins consist of three subunits designated $\alpha, \beta,$ and $\gamma$. The $G_{\alpha}$ subunit is a GTPase switch protein that cycles between active and inactive states depending on whether it is bound to GTP or to GDP. Review the steps for ligand-induced activation of effector proteins mediated by the trimeric G proteins. Suppose that you have isolated a mutant $G_{\alpha}$ subunit that has an increased GTPase activity. What effect would this mutation have on the G protein and the effector protein?
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