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Which of the following regarding GPCR's is FALSE?
GPCR ligand binding stimulates phosphorylation of the heterotrimeric G protein
GPCR's have seven transmembrane domains
The alpha subunit of the heterotrimeric G protein is active in its GTP bound state
The beta-gamma subunit of the heterotrimeric G protein performs signaling functions
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- Cholera toxins, produced by the pathogenic bacteria Vibrio cholerae, disrupt G Protein Coupled Receptor (GPCR) signaling pathways. They interfere with... the ability of the beta subunit of a G protein to bind to the GPCR the ability of the gamma subunit of a G protein to exchange GDP for GTP the ability of the beta subunit of a G protein to bind to an effector protein the ability of the alpha subunit of a G protein to hydrolyze GTP to GDPLigand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below 1) Which of the proteins demonstrate the tightest/strongest binding of the hormone? Which demonstrates the least tight binding of the hormone? What is the basis for your answer?Ligand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.
- In the case of GPCR (G protein coupled receptor) signaling pathways, which of the following statements is INCORRECT? The gamma subunit of the trimeric G protein has a transmembrane domain whereas the alpha and beta subunits are peripheral proteins If G alpha was locked in a GTP bound state, it would be bound to the effector enzyme rather than to the beta and gamma subunits. In some but not all signaling pathways, when the beta and gamma subunits are separated from alpha - the beta/gamma pair can also stimulate the activation of effectorsDuring the epinephrine signaling pathway we learned about in class, the enzyme glycogen phosphorylase is regulated by: Allosteric regulation Covalent modification Competitive inhibition Zymogen activationThe 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.
- Most of the GLP-1 receptor structure form part of the transmembrane domain (TMD) that is embedded in the plasma membrane. The TMD enables the transmission of signal induced by the binding of GLP-1 from outside the cell into the cytoplasm of the cell, which in turn initiates a signaling cascade that ultimately leads to insulin secretion. Is the TMD of the receptor mainly hydrophobic or hydrophilic? Explain your answer in 1 – 3 sentences.An SH2-containing protein contains a mutation that changes its binding pocket such that tyrosine and phosphotyrosine bind with equal affinity. As a result, MEK activity: does not change with receptor dimerization and transautophosphorylation decreases due to changes in Raf activation increases with ligand binding-induced dimerization decreases due to allosteric inhibition of SH2-domain bindingSignaling activity of G proteins is controlled by GTPase activating proteins (GAPs) and Guanine exchange factors (GEFs). What are the mechanisms by which GAPS and GEFs control G protein functions? GEFS inhibit G protein functions by stimulating GTP hydrolysis; GAPs activate G protein functions by stimulating GDP-GTP exchange. O GAPS inhibit G protein functions by stimulating GTP hydrolysis; GEFs activate G protein functions by stimulating GDP-GTP exchange. GEFS inhibit G protein functions by stimulating GTP hydrolysis; GAPS activate G protein functions by inhibiting GDP-GTP exchange. GAPs stimulate G protein functions by blocking GTP hydrolysis; GEFS inhibit G protein functions by stimulating GTP-GDP exchange. GAPS inhibit G protein functions by stimulating GDP-GTP exchange; GEFS activate G protein functions by stimulating GTP hydrolysis
- When a trimeric G protein is activated by GPCR? The three subunit of the G protein remain tightly associated with each other; the GDP bound to the a subunit is phosphorylated to form bound GTP; it dissociates into a free B subunit and an ay subunit Options: hydrolyzed, cleaves, phosphorylate, dephosphorylates, folds, glycosates; gtp, gdp, cgmp, atp, adp, camp; cleaves, phosphorylation, dephosphorylation, unfolds, glcosylates, deglycosylate; leucine kinases, glycine kinase, Tyrosine kinases, valine kinase; triimetization, dimerization, monomerizationPathway 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 portionSome strains of bacteria or microorganisms have developed toxins that can modify the activity of the alpha subunit of G proteins which results in disease. For ex. cholera toxin, produced by Vibrio cholerae, causes ADP ribosylation of the stimulatory Gαs subunit of G proteins. This modification abolishes the GTPase of Gαs, and results in an αs subunit that is always in the “on” or active state. It results in continuous stimulation of adenylyl cyclase (AC). The main cells affected by this are the epithelial cell in gastrointestinal tract. Knowing this altered activity of AC, explain why patients affected by this toxin experience severe diarrhea and dehydration that may result in death.