PKA is activated after its regulatory subunit is dissociated from the catalytic subunit. Select one: O True O False
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- You perform a competition study on a GPCR. You have isolated the plasma membrane from cells which contains the GPCR of interest. If an agonist and an inverse agonist are at equal concentrations in your study but the inverse agonist has a 10 x higher affinity for the receptor than the agonist, what would you expect to be the overall outcome to be? More of the agonist is bound and so most of the receptor is in its active conformation and is stimulated More of the inverse agonist is bound and so most of the receptor is in its inactive conformation and is unstimulated.Name three features common to the activation of cytokine receptors and receptor tyrosine kinases. Name one difference with respect to the enzyme activity of these receptors.Upon activation by a receptor, a G protein exchanges bound GDP for GTP, rather than phosphorylating GDP that is already bound. Similarly, the a subunit-GTP complex has a slow GTPase activity that hydrolyzes bound GTP, rather than exchanging it for GDP. Describe experimental evidence that would be consistent with these conclusions.
- AMPK and mTOR can both be considered intracellular signal integrators. Explain this definition.added ligand concentration of 10 µM is 5 × 10³ s¹. What is the value of the reverse rate constant k_1 = 1 ×10-4 Incorrect Macmillan Learning You have not correctly calculated the value of the reverse rate constant. To begin, calculate the value of k₁ by dividing the rate of receptor-ligand complex formation (the rate of the forward reaction) by the ligand concentration. k₁ = rate forward [L] Then, calculate the value of the reverse rate constant, k_₁, by multiplying the dissociation constant, Kd, and the forward rate constant, k₁. k_1 = Kak₁When protein kinase A (PKA) is inactive, which of the following statements is true? ATP is bound to the regulatory subunit to inhibit subunit dissociation. CAMP is bound to the catalytic site to inhibit the regulatory subunit. The regulatory subunit has cyclic GMP bound in place of cyclic AMP. The intrinisic pseudosubstrate peptide is bound to the active site.
- Pay close attention to the information related to figure 3.14a and the structure of the PKA catalytic site in this figure. In a few well-written sentences, propose the following: A mutation that would result in PKA becoming a dead kinase*. A mutation that would result in PKA becoming a constitutively active** kinase.Arrange following the boxed information in sequence regarding the dissociation and reassociation of G proteins following the activation of a G protein coupled receptor. GTP-bound Ga, dissociates from B and y cuhunits Gas exchanges GTP for GDP Gas reassociates with By subunits and the rorentor reforms Binding of the ligand to a G-protein rounled recentor GTP-bound Gas binds and activates adenvlul rurlase GTP is hydrolyzed and GDP bound Gas suhunit dissoriates Conformational change Increased synthesis of CAMP from ATPPathway divergence occurs when: signaling pathways use a common intermediate one signaling pathway triggers another O signaling pathways produce the same outcome signaling pathways split to produce multiple outcomes Question 8 Where are receptor tyrosine kinases usually phosphorylated? O tyrosine residues in the allosteric regulatory portion tyrosine residues in the N-terminal portion tyrosine residues in the transmembrane portion O tyrosine residues in the C-terminal portion
- The G protein coupled receptor (GPCR) pathway elicits diverse intracellular responses in different cells. The basic steps of GPCR signaling are outlined in this diagram. Which of the following statements correctly describes the process of GPCR signaling? The GPCR activation is reversible after the signal of the ligand diminishes. The membrane-embedded enzyme uses GTP as a secondary messenger to initiate gene expression. The ligand attaches to both the GPCR and the membrane-embedded enzyme to activate the GPCR pathway. The ligand-bound GPCR sends a GTP molecule to an enzyme in the membrane and switches it into an active state.During the epinephrine signaling pathway we learned about in class, the enzyme glycogen phosphorylase is regulated by: Allosteric regulation Covalent modification Competitive inhibition Zymogen activationsignal amplification of cells relies on which of hte following increased activity of protein phosphatases sequential increase in the different components, wherein a single, activated component can activate many copies of the next component in the pathway increasing numbers of cell-surface receptors as the signal is transduced increasing amounts of ligand aas signal transdutciton proceeds