Binding EGF to the EGF receptor causes phosphorylation of tyrosines on the cytoplasmic tail of the receptor. Which of the following best describes the mechanism by which this phosphorylation activates downstream signaling complexes? Select one A. Causes degradation of receptor by proteasome pathway B. Causes EGF receptor to be internalized so it can interact directly with downstream signaling molecules C. Tyrosine phosphorylation alters 3D structure of downstream signaling proteins causing them to change from an inactive to active conformation D. Causes release of EGF from receptor E. Alters the localization of downstream signaling partners in the cytoplasm

Binding EGF to the EGF receptor causes phosphorylation of tyrosines on the cytoplasmic tail of the receptor. Which of the following best describes the mechanism by which this phosphorylation activates downstream signaling complexes? Select one A. Causes degradation of receptor by proteasome pathway B. Causes EGF receptor to be internalized so it can interact directly with downstream signaling molecules C. Tyrosine phosphorylation alters 3D structure of downstream signaling proteins causing them to change from an inactive to active conformation D. Causes release of EGF from receptor E. Alters the localization of downstream signaling partners in the cytoplasm

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter6: Cell Communication

Section: Chapter Questions

Problem 8TYU: Scaffold proteins (a) release kinases and phosphatases into the extracellular fluid (b) bind G...

See similar textbooks

Similar questions

Activation of certain GPCRs triggers an intracellular signaling mechanism that involves activation of adenlyl cyclase and an increase of cAMP. Which of the following statements best describes the the events that follow such a cAMP increase? a.) The cAMP increase leads to activation of protein kinase C. b.) The cAMP increase leads to activation of the release of the gamma subunit from the GPCR. c.) The cAMP increase leads to activation of protein kinase A.
TAS2R38 codes for a G-protein coupled receptor which contributes to the tasting of PTC. What does this tell you about PTC as a type of ligand? a It is a protein-based ligand that can cross the CM into the cell b It is a lipid based ligand that can cross the CM into the cell c It is a protein-based ligand that requires a second messenger d It is a lipid-based ligand that requires a second messenger
Even in the presence of a Ras-GAP, a single amino acid change in as renders it incapable of hydrolyzing GTP. This mutation is known as Ras+ and is a cancer-causing mutation. What effect do you think this mutation will have on signaling downstream of Ras+? Why? a)A mutation would turn on the signaling pathway all of the time. b)Even if a route is mutated, it can still be turned on or off. c)Due to a mutation, the signaling pathway would always be off.
You stimulated the cell with a ligand and analyzed the response. Upon ligand treatment, the cell increased the expression of gene α and decreased expression of gene β. When you inhibit cyclic AMP production by treating the cell with an inhibitor of Adenylyl cyclase, the increased expression of gene α was not observed but the decrease gene β expression was still observed. a) What you can expect for gene α regulation by this ligand? What signaling mechanism could be used? b) To determine how gene β is regulated by the ligand via what signaling mechanism, provide your hypothesis and indicate a potential experiment that you can perform to test that.
Compare and contrast GPCR and RTK signaling. What role does GTP play in each? What role does phosphorylation play? How is each signal differently amplified? How do these two signaling types compare to steroid signaling with respect to gene activation?
You are studying a drug that affects a cAMP signalling pathway that is normally initiated when a signalling molecule binds to a G-protein coupled receptor. You determine that the drug prevents the hydrolysis of GTP bound to G-proteins in this pathway. Describe the impact, if any, that this drug would have on the G-protein coupled receptor (GPCR), assuming that the pathway has been activated by the presence of the signalling molecule (first messenger). Include an explanation for your response.
List three ways in which a signal is amplified in a Gprotein-coupled receptor signaling pathway.
When insulin binds to its receptor, a conformational change occurs that results in auto phosphorylation of the receptor on a specific Tyr residues. In the next step of the signaling pathway, an adaptor protein called IRS-1(insulin receptor substrate-1) docks with the phosphorylated receptor. This step is essential for the downstream activation of several kinases including Alk, also known as protein B as well as protein C kinase and GSK-3. Protein kinase 3 is involved in mobilizing GLUT 4 glucose transporters to the plasma membrane and GSK-3 phosphorylates glycogen sunthase. What would be the effects of a mammalian organism over expressing IRS-1 were also deficient in muscle GAK-3? Would this deficiency be lethal ?
Compare and contrast GPCR and RTK signaling. What role does GTP play in each? What role does phosphorylation play? How do these two signaling types compare to steroid signaling with respect to gene activation?
Imagine a disease that involves reduced expression of receptor X. There is no concentration of full agonist that can restore receptor X signaling back to normal levels. Explain how an allosteric modulator may be used to help in this situation.
The hypothesis for the experiment shown in the picture is that the TamC3 and TamR3 cell lines function, and grow the absence of estrogen, receptor function. Reduced reliance on estrogen, receptor signaling alters mTOR pathway activity. If this hypothesis is true, then mediators of mTOR signaling (Akt or p70S6K) should have reduced levels of phosphorylation . A. Where would you look to see this? B. To what degree does the data in the picture support the hypothesis?
A scientist observes a mutation in the transmembrane region of EGFR that eliminates its ability to be stabilized by binding interactions during dimerization after ligand binding. Which hypothesis regarding the effect of this mutation on EGF signaling is most likely to be correct? a. EGF signaling cascades would be active for longer in the cell. b. EGF signaling cascades would be active for a shorter period of time in the cell. c. EGF signaling cascades would not occur. d. EGF signaling would be unaffected.

SEE MORE QUESTIONS

Recommended textbooks for you

Biology (MindTap Course List)

Biology

ISBN:

9781337392938

Author:

Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:

Cengage Learning

Biology (MindTap Course List)

Biology

ISBN:

9781337392938

Author:

Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS

GET THE APP

About FAQ Academic Integrity Sitemap Document Sitemap

Contact Bartleby Contact Research (Essays)High School Textbooks Literature Guides Concept Explainers by Subject Essay Help Mobile App

GET THE APP

Privacy

Your CA Privacy Rights

Your NV Privacy Rights

About Ads

Manage My Data

bartleby, a Learneo, Inc. business

	A.	Causes degradation of receptor by proteasome pathway
	B.	Causes EGF receptor to be internalized so it can interact directly with downstream signaling molecules
	C.	Tyrosine phosphorylation alters 3D structure of downstream signaling proteins causing them to change from an inactive to active conformation
	D.	Causes release of EGF from receptor
	E.	Alters the localization of downstream signaling partners in the cytoplasm