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

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter4: Principles Of Neural And Hormonal Communication

Section: Chapter Questions

Problem 14RE: A common membrane-bound intermediary between the receptor and the effector protein within the plasma...

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Ligand binding of a (????) causes conformational changes in the receptor that free the associated G-protein to interact with other membrane proteins Voltage gated ion channel GPCR Ligand gated ion channel Ligandase pore
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
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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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
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 ATP
Which statement best describes the interaction that occurs as a result of the binding of a ligand to a ligand-gated ion channel receptor? A B с D ligand extracellular environment gate closed inactive ligand-gated ion channel receptor ions The process permanently opens or closes the ion channel. cytoplasm The process alters the membrane potential by changing the intracellular ionic concentration. The process causes G proteins to bind with GTP and become activated. The process removes three sodium ions from the cell and brings in two potassium ions.