Suppose you were investigating a newly discovered growth-factor signal-transduction pathway, involving a G-protein-coupled receptor system. When you add GTP$\gamma$S, a nonhydrolyzable analog of GTP, the duration of the hormonal response increased. Why does the response last longer in the presence of GTP$\gamma$S? O G$\alpha$ binds covalently to adenylate cyclase in the presence of GTP$\gamma$S. O GTP$\gamma$S prolongs the G$\alpha$-adenlylate cyclase association because GDP formation cannot occur. O The G$\alpha$-GTP$\gamma$S complex has higher affinity for the $\beta\gamma$ dimer (G$\beta\gamma$) than for adenylate cyclase. O Adenylate cyclase binds to GTP$\gamma$S independently of the G protein. O The G protein in this signal-transduction pathway is defective for nucleotide binding.
Added by Charlotte W.
Close
Step 1
This means that GTP$\gamma$S binds to the G protein but cannot be hydrolyzed to GDP, which is the normal mechanism for inactivating the G protein. Show more…
Show all steps
Your feedback will help us improve your experience
Suman K and 84 other Biology educators are ready to help you.
Ask a new question
Labs
Want to see this concept in action?
Explore this concept interactively to see how it behaves as you change inputs.
Key Concepts
Recommended Videos
Suppose a researcher discovers a new growth-factor signal-transduction pathway. When the researcher adds the nonhydrolyzable GTP analog GTP̳S, the duration of the hormonal response increases. Why does the hormonal response last longer in the presence of GTP̳S? Ga binds covalently to adenylate cyclase in the presence of GTP̳S. The Ga-GTP̳S complex has a higher affinity for G̢ and G̳ than for adenylate cyclase. GTP̳S prolongs the Ga-adenylate cyclase association because GDP formation cannot occur. Adenylate cyclase binds to GTP̳S independently of the G protein. The G protein in this signal-transduction pathway is defective for nucleotide binding.
Suman K.
You mutate a heterotrimeric G protein so that the alpha subunit can no longer dissociate from the beta and gamma subunits. How would this mutation affect G protein-coupled receptor (GPCR) signaling? - The signal transduction pathway would activate normally but be unable to terminate properly. - Cyclic AMP levels would rise uncontrollably. - Adenylyl cyclase would remain activated. - The signal transduction pathway could not activate in response to ligand binding. - The ligand would not bind to the GPCR.
Bryan V.
How does the presence of the poorly hydrolyzable GTP analog GTP $\gamma$ S (in which an $O$ atom on the terminal phosphate is replaced by an $\mathrm{S} \text { atom })$ affect cAMP production by adenylate cyclase?
Recommended Textbooks
Biology for AP Courses
Objective Biology for NEET
Introduction to General, Organic and Biochemistry
Transcript
Watch the video solution with this free unlock.
EMAIL
PASSWORD