G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) are two basic receptor types by which cells transduce signals. Classify each statement as describing GPCRs, RTKs, both types of receptors, or neither. GPCRs structure contains seven transmembrane helices activate heterotrimeric G proteins directly transports some ligands through the membrane an example is the epinephrine receptor RTKs Both receptor activation causes phosphorylation of its cytosolic subunits phosphorylation of receptor can an example is the terminate signal or insulin receptor desensitize receptor autophosphorylation of receptor can initiate signal ligand binding induces conformational change in receptor Incorrect Answer Answer Bank Neither

G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) are two basic receptor types by which cells transduce signals. Classify each statement as describing GPCRs, RTKs, both types of receptors, or neither. GPCRs structure contains seven transmembrane helices activate heterotrimeric G proteins directly transports some ligands through the membrane an example is the epinephrine receptor RTKs Both receptor activation causes phosphorylation of its cytosolic subunits phosphorylation of receptor can an example is the terminate signal or insulin receptor desensitize receptor autophosphorylation of receptor can initiate signal ligand binding induces conformational change in receptor Incorrect Answer Answer Bank Neither

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter9: Cell Communication

Section: Chapter Questions

Problem 1VCQ: Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is...

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Select statements that accurately describe receptor tyrosine kinases (RTKs). Some RTKs are dimeric in the presence of a ligand. GTPase activity is required for autophosphorylation (cross-phosphorylation). The structure includes a transmembrane helix. The intracellular domain has kinase domains. The a subunit contains seven a helices that span the membrane. A ligand binds to the extracellular domain.
Would an extracellular signal receptor protein mostly likely consist of type 1 or type 2 alpha helices? Explain your reasoning
b) Complete the following flow chart| (a membrane phospholipid)_ Hydrolysed by phospholipase C, to produce Remains associated with plasma membrane a small polar molecule released to cytosol, diffuses to the iv. and causes the release of v. by binding to receptors that are ligand-gated channels. Activates other proteins Activates vi which then phosphorylates other intracellular targets. form complex with vii.
The Structure of the acetylcholine receptor is shown below: A. Knowing the amino acid sequence of this protein, what tool would you use to identify the membrane-spanning region? Explain how it works.
Pathway 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
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An analog of cGMP, 8-Br-cGMP, will permeate cellular membranes, is only slowly degraded by a rod cell’s PDE activity, and is as effective as cGMP in opening the gated channel in the cell’s outer segment. If you suspended rod cells in a buffer containing a relatively high [8-Br-cGMP], then illuminatedthe cells while measuring their membrane potential, what would you observe?
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Explain why this is not true about ion channel receptors; It forms hydrophobic hollow because it is a membrane bound receptor.
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.
Cytokine receptors and tyrosine kinase receptors are similar in all of the following ways EXCEPT one. Which one is the exception? O They are both down-regulated by lysosomal degradation They both involve receptor exoplasmic domain dimerization They both result in an effector protein entering the nucleus O They both involve cytosolic domain phosphorylation
In the two competition study experiments below, what can you say about the relative affinities of the labeled ligand and the unlabeled competitor ligand? Remember to check the concentrations of both in each experiment. extracellular plasma membrane intracellular Competition study Competitor unlabeled ligand Labeled ligand †††† Receptor 10 nM Competitor unlabeled ligand 10 nM Labeled ligand ŸŸŸŸ 9 nM Competitor unlabeled ligand 3 nM Labeled ligand