Warning: foreach() argument must be of type array|object, bool given in /var/www/html/web/app/themes/studypress-core-theme/template-parts/header/mobile-offcanvas.php on line 20

Cells can terminate signal transduction by cell surface receptors by A. reducing agonist availability in the vicinity of the target cell. B. internalizing and degrading the receptor-agonist complex. C. modifying the receptor so that it is inactive or desensitized. D. all of the above. E. none of the above.

Short Answer

Expert verified
Answer: All of the above (A, B, and C). Cells can terminate signal transduction by reducing agonist availability, internalizing and degrading the receptor-agonist complex, and modifying the receptor to make it inactive or desensitized.

Step by step solution

01

Understand the Cell Surface Receptor-Signal Transduction Process

First, it's essential to have a basic understanding of the cell surface receptor-signal transduction process. Cell surface receptors are proteins that help transmit signals across the cell membrane. These signals are typically initiated by extracellular molecules (agonists) that bind to the receptor. This binding event triggers a cascade of intracellular signaling events, which ultimately affect cellular processes and functions.
02

Analyze Option A - Reducing Agonist Availability

Option A suggests that signal transduction termination can occur by reducing the availability of the agonist near the target cell. This is accurate, as reducing the concentration of the signaling molecule would decrease the probability of binding and initiating the signal transduction process.
03

Analyze Option B - Internalizing and Degrading the Receptor-Agonist Complex

Option B states that internalizing and degrading the receptor-agonist complex can terminate signal transduction. This is also true. When the receptor-agonist complex is internalized, the signaling process is interrupted. Within the cell, the complex can be degraded, separating the agonist and receptor to end the current signaling event.
04

Analyze Option C - Modifying the Receptor

Option C mentions that modifying the receptor to make it inactive or desensitized can terminate signal transduction. This is also accurate. Cellular processes such as phosphorylation can lead to receptor desensitization or inactivation. When a receptor is desensitized or inactive, it is unable to initiate or transmit signals, effectively terminating the signal transduction.
05

Determine the Correct Answer

As we have analyzed each of the statements A, B, and C, we have discovered that all of them are accurate mechanisms through which cells can terminate signal transduction by cell surface receptors. Therefore, the correct answer is option D, which states "all of the above."

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Over 30 million students worldwide already upgrade their learning with Vaia!

Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Cell Surface Receptors
Understanding signal transduction is rooted in understanding cell surface receptors, which are crucial for the communication of cells with their external environment. Imagine these receptors like radio antennas that catch specific signals—in the body, these signals are chemical messengers, or agonists, like hormones, neurotransmitters, and other signaling molecules.

Once an agonist is detected by these receptors, the cell surface receptor undergoes a conformational change. This shape-shift starts a sequence of reactions inside the cell, known as a signaling cascade. It's as if the cell suddenly wakes up and gets to work, executing specific instructions encoded by the signal. In a way, cell surface receptors can be seen as the translators of external messages into internal actions that maintain the body's balance and respond to changes in the environment.
Agonist Availability
The 'conversation' a cell has with its environment can be muted by decreasing the availability of the agonist, akin to lowering the volume on a loudspeaker. Agonist availability refers to the presence of those chemicals that bind to receptors to initiate a signal.

If the concentration of an agonist around a target cell drops, maybe due to enzymes breaking the agonist down or by its uptake into other cells, the chance of it binding to a cell's receptors plummets. This would effectively interrupt the signal transduction. Without an agonist, the receptor remains 'off,' so to speak, waiting for the next signal that may or may not come.
Receptor-Agonist Complex
When an agonist and receptor come together, they create what's known as a receptor-agonist complex. This complex is the starting gun for the signaling cascade. However, the body has a neat trick: after a cell 'reads' the signal's message, it can take this complex inside itself, a process called endocytosis, and then dismantle it.

This is where a cell's internal recycling system comes into play—breaking down the complex to either reuse the parts or dispose of them entirely. It's as if the cell has a 'read and shred' policy for some messages to ensure those signals stop when they have served their purpose, thus preventing overactivity that could lead to cellular chaos.
Receptor Desensitization
Like people tuning out a repetitive noise, receptors can also become unresponsive or 'tired' after being exposed to the same signal for too long, a process known as receptor desensitization. Desensitization can happen through several mechanisms, such as phosphorylation, where a phosphate group is added to the receptor to change its shape and functionality.

In this changed state, the receptor no longer listens to its regular agonist, essentially muting the signal. This is how the body regulates overly prolonged or intense signals, safeguarding cells from excessive stimulation and maintaining homeostasis—a stable and balanced internal environment.

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

The ErbB/HER family of receptor tyrosine kinase genes are linked to many different types of human cancers. Overexpression of any of these genes would lead to an increase in the various receptors. ErbB2 encodes the HER2 protcin. This receptor does not bind any known extracellular growth factor, but it does form dimers with other growth-factor-bound HER receptors. Even modest overexpression of HER2 can alter normal cell growth regulation. Ras protein is a critical regulator in cell proliferation, and its activity is enhanced by activated tyrosine kinase. Elements of its action include all of the following except A. formation of cyclic GMP. B. adaptor proteins binding to phosphorylated ryrosines on receptor tyrosine kinase. C. recruitment and stimulation of Ras-activating protein. D. exchange of GDP for GTP on the Ras protein. E. initiation of a cascade in which several kinases are activated sequentially by phosphorylation.

The ErbB/HER family of receptor tyrosine kinase genes are linked to many different types of human cancers. Overexpression of any of these genes would lead to an increase in the various receptors. ErbB2 encodes the HER2 protcin. This receptor does not bind any known extracellular growth factor, but it does form dimers with other growth-factor-bound HER receptors. Even modest overexpression of HER2 can alter normal cell growth regulation. Which of the following statements about receptor tyrosine kinases is correct? A. The catalytic domain is on the N-terminal end. B. Activation of the kinase requires ATP. C. Growth factor binding to the receptor triggers dimerization which activates the kinase activity. D. Active tyrosine kinase can phosphorylate other proteins but not itself. E. All of the above.

Calmodulin is A. a nonspecific kinase. B. a protein that binds \(\mathrm{Ca}^{2+}\). C. a second messenger. D. an activator of nitric oxide synthase. E. a protein channel that facilitates the influx of \(\mathrm{Ca}^{2+}\).

Intracellular receptors A. usually bind hydrophobic ligands. B. may be located either in the cytosol or nucleus in unbound state. C. when bound to their ligand, regulate gene transcription. D. when bound to their ligand, function as dimeric complexes binding to specific DNA sequences. E. all of the above.

Growth hormone releasing hormone (GHRH) produced by the hypothalamus binds to its pituitary receptor and leads to the production of growth hormone (GH) because of increase in cyclic AMP. Certain pituitary tumors result in hypersecretion of GH because of a mutation that produces a \(G_{s}-\alpha\) protein with a greatly diminished GTPase activity. Low GTPase activity in the mutated protein results in consitutive activation of \(G_{s}\) and adenylate cyclase because A. GTP-bound \(\alpha\) -subunit does not reform the \(\alpha \beta \gamma\) trimer. B. GTP-bound G protein binds more strongly to the membrane receptor. C. GTP reacts directly with adenylate cyclase to activate it. D. the trimeric form of the G protein is stabilized. E. adenylate cyclase is phosphorylated more readily.

See all solutions

Recommended explanations on Chemistry Textbooks

View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.

Sign-up for free