Biology 11th Edition Raven Test Bank Download

Chapter 09 - Cell Communication
Test Bank for Biology 11th Edition by

Raven Johnson Mason Losos and
Singer
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Chapter 09
Cell Communication
Multiple Choice Questions
1. The protein Sonic Hedgehog (SHH) plays a role in specifying the identity of digits (such
as fingers and toes) in mammals. Several digits arise directly from cells that both express and
respond to secreted SHH. What type of signaling would this be considered?
A. Direct contact
B. Paracrine
C. Endocrine
D. Synaptic
E. Autocrine
If a cell responds to the ligand that it secretes, this is considered autocrine signaling.
Blooms Level: 2. Understand

Gradable: automatic
LO: 09.01.01 Discriminate between methods of signaling based on distance from source to reception.
Section: 09.01
Topic: Overview of Cell Communication
9-1
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McGraw-Hill Education.
2. One cell sends second messengers to another cell through gap junctions. What type of
signaling would this be considered?
A. Direct contact
B. Paracrine
C. Endocrine
D. Synaptic
E. Autocrine
Gap junctions require direct contact between cells, and thus this is an example of direct
contact signaling.
Blooms Level: 1. Remember

Gradable: automatic
Section: 09.01
3. In synaptic signaling, neurotransmitters are released into a space that is referred to as a:
A. chemical synapse.
B. neuron junction.
C. paracrine space.
D. gap junction.
E. plasmodesmata.

Gradable: automatic
Section: 09.01
9-2
4. In response to injury, cell fragments called platelets get activated to induce clotting.
Activated platelets release factors that can in turn bind to specific membrane receptors on
nearby cells. What type of signaling would this be considered?
A. Direct contact
B. Paracrine
C. Endocrine
D. Synaptic
E. Autocrine
Since the factors are acting on cells in the local environment, this is an example of paracrine
signaling.

Gradable: automatic
Section: 09.01
9-3
5. A researcher is working to generate a new cancer drug. Thus far, he has identified a
compound that can reduce the size of tumors in the lung. However, in order for the drug to
work, the lung tumor has to be small. In addition, the tumor cannot have metastasized (spread
to other areas of the body). Furthermore, he knows that the drug acts to prohibit the signaling
from one tumor cell to another tumor cell. Given the above information, this new drug
prohibits:
A. synaptic signaling between tumor cells.
B. autocrine signaling between tumor cells.
C. paracrine signaling between tumor cells.
D. endocrine signaling between tumor cells.
Clarify Question
• What is the key concept addressed by the question?

o The question asks about signaling involved in cancer growth.
• What type of thinking is required?
o You are being asked to analyze the signaling involved in cancer growth.
Gather Content
• What do you know about signaling involved in cancer growth? What other information is
related to the question?
o Synaptic signaling occurs between neurons across a synapse. Autocrine signaling is a
cell talking to itself. Endocrine signaling involves hormones that travel through the blood to
act on different organs. Paracrine signaling involves communication with nearby cells.
Choose Answer
• Given what you now know, what information is most likely to produce the correct
answer?
o Since the drug only works on small tumors that have not metastasized, and prevents
signaling from one cell to another cell, it must inhibit paracrine signaling. Synaptic signaling
is irrelevant in this case, as signaling does not involve neurons.
Reflect on Process
• Did your problem-solving process lead you to the correct answer? If not, where did the
process break down or lead you astray? How can you revise your approach to produce a
more desirable result?
o This question asked you to analyze the signaling involved in cancer growth. If you got
the correct answer, great job! If you got an incorrect answer, where did the process break
down? Did you think that synaptic signaling would stimulate growth in a cell? Did you think
that endocrine signaling worked on nearby cells?
9-4
Blooms Level: 4. Analyze

Gradable: automatic
Section: 09.01
9-5
6. Using a specific chemical, a cell biologist has blocked one type of channel-linked
receptor in a lab rat's liver tissue. What was the likely mechanism of the chemical she used?
A. The chemical prohibits binding of a ligand to the receptor.
B. The chemical prohibits ions from entering the cell via active transport.
C. The chemical causes ions to move in the opposite direction of the ion gradient.
D. The chemical prohibits second messenger signaling.
Clarify Question

o The question asks about specifically inhibiting one class of receptors.
o You are being asked to apply your knowledge about specifically inhibiting one class
of receptors.
Gather Content
• What do you know about specifically inhibiting one class of receptors? What other
information is related to the question?
o Receptors bind to specific ligands. This then can activate the opening of ion channels
or production of second messengers. Multiple receptors can activate similar pathways, but
only one ligand binds each receptor.
Choose Answer
answer?
o To specifically inhibit one receptor a chemical that binds to the ligand binding site
would work best. Chemicals that block the movement of ions do not specifically block the
action of one receptor.
Reflect on Process
o This question asked you to apply your knowledge about specifically inhibiting one
class of receptors. If you got the correct answer, great job! If you got an incorrect answer,
where did the process break down? Did you think that blocking movement of ions would be
specific to one receptor? Did you think that ion transport would use second messenger
signaling?
9-6
Blooms Level: 3. Apply

Gradable: automatic
LO: 09.02.01 Contrast the different types of receptors.
Section: 09.02
Topic: Receptor Types
9-7
7. Leptin is a circulating hormone that is produced by fat cells and plays a role in body
metabolism and obesity. It normally binds to receptors in the brain and inhibits
appetite. Studies have demonstrated that when obese mice that are leptin deficient are injected
with leptin they quickly lose their excess weight. Interestingly, however, many overweight
people have high levels of leptin in their bloodstream. Why do you think that the high levels
of leptin in obese individuals are insufficient to curb their appetite?
A. Paracrine signaling may be disrupted in obese people with high levels of leptin.
B. Obese people who have high levels of leptin may have a leptin receptor with decreased
sensitivity.
C. The form of leptin released by obese people may lack protein kinase activity.
D. In obese people with high levels of leptin, the leptin is a non-functional second messenger.
9-8
Clarify Question

o The question asks about resistance to leptin.
o You are being asked to analyze why some obese people are resistance to leptin.
Gather Content
• What do you know about resistance to leptin? What other information is related to the
question?
o For a hormone like leptin to function it must bind to a receptor. This then allows a
signal to pass into the cell. If the hormone levels are low, or the receptor does not work
properly then the cells do not respond to the hormone.
Choose Answer
answer?
o If a person lacks leptin or the receptor then their brain will not receive a signal that
they are full and their appetite will not be inhibited. Obese individuals who have normal leptin
levels but low leptin receptor activity will not respond to the leptin, will be hungry more often
and become obese.
Reflect on Process
o This question asked you to analyze why some obese people are resistance to leptin. If
you got the correct answer, great job! If you got an incorrect answer, where did the process
break down? Did you think that leptin was a paracrine signal instead of endocrine? Did you
think that leptin was a second messenger or kinase?

Gradable: automatic
Section: 09.01
9-9
8. Vasopressin is a hormone that is primarily released when the body is low on water.
Release of vasopressin causes the kidneys to conserve water by concentrating urine and
decreasing urine output. However, vasopressin also has additional functions in other tissues
such as the brain and blood vessels, which are not directly involved in urine production. How
could it be possible for vasopressin to trigger different responses in different tissues?
A. Vasopressin can bind to, and act on, different receptor subtypes, leading to different
cellular responses in different tissues.
B. Vasopressin can be released at different times to result in different effects.
C. Vasopressin binds to the same exact receptor in different tissues, but causes a different
conformational change to the receptor in each tissue.
D. The kidneys have a receptor for vasopressin, but cells in the brain and blood vessels do
not have a receptor for vasopressin.

Gradable: automatic
LO: 09.01.02 Describe how phosphorylation can affect protein function.
Section: 09.01
9-10
9. Addison's disease is a disorder that results from a reduction in production of

glucocorticoids and mineralocorticoids. Individuals with Addison's disease suffer from a
variety of systemic symptoms including: muscle weakness, fever, issues with the
gastrointestinal tract, and increased tanning. Considering this information, what type of
signaling do you think that glucocorticoids and mineralocorticoids stimulate?
A. Direct contact
B. Paracrine
C. Endocrine
D. Synaptic
E. Autocrine
9-11
Clarify Question

o The question asks about different types of signaling.
o You are being asked to analyze what type of signaling glucocorticoids and
mineralocorticoids perform.
Gather Content
• What do you know about different types of signaling? What other information is related
to the question?
o Signaling with adjacent cells include paracrine, direct contact, synaptic and autocrine.
Endocrine signaling works at a distance with the hormones moving through the blood to
distant organs.
Choose Answer
answer?
o Since the symptoms of this disease are systemic and occur throughout the body, this is
an example of endocrine signaling. In fact, glucocorticoids and mineralocorticoids are
hormones, and this disease is considered an endocrine disorder.
Reflect on Process
o This question asked you to analyze what type of signaling glucocorticoids and
mineralocorticoids perform. If you got the correct answer, great job! If you got an incorrect
answer, where did the process break down? Did you think that by affecting many organs
glucocorticoids and mineralocorticoids only worked on nearby cells? Did you think that
glucocorticoids and mineralocorticoids were not hormones?

Gradable: automatic
Section: 09.01
9-12
10. What is the function of a protein kinase?

A. To remove phosphate groups from proteins
B. To cleave membrane phospholipids
C. To phosphorylate GDP to generate GTP
D. To add phosphate groups onto proteins
Protein kinases phosphorylate proteins

Gradable: automatic
Section: 09.01
9-13
11. You have identified a novel cytoplasmic protein. Through sequence analysis you are able
to identify the presence of a number of serine/threonine phosphorylation motifs. Based on
these data, you hypothesize that this protein may be a substrate for what kind of enzyme?
A. A protein kinase
B. A receptor tyrosine kinase
C. A G protein-coupled receptor
D. A tyrosine phosphatase
E. A phospholipase
Clarify Question

o The question asks about phosphorylation of a protein.
o You are being asked to apply your knowledge about phosphorylation of a protein.
Gather Content
• What do you know about phosphorylation of a protein? What other information is

related to the question?
o The class of enzyme that adds phosphate groups from ATP to proteins is called a
protein kinase. These phosphate groups can be added to the three amino acids that have an
OH as part of their R group, namely serine, threonine, and tyrosine. We categorize protein
kinases as either serine–threonine or tyrosine kinases based on the amino acids they modify.
Most cytoplasmic protein kinases fall into the serine–threonine kinase class.
Choose Answer
answer?
o Since this protein has serine/threonine phosphorylation motifs, it may be a substrate
for serine/threonine phosphatases and kinases. Phospholipases cleave phospholipids. GPCRs
are not enzymes. Phosphatases remove phosphates from proteins.
Reflect on Process
o This question asked you to apply your knowledge about phosphorylation of a protein.
If you got the correct answer, great job! If you got an incorrect answer, where did the process
break down? Did you think that the serine/threonine phosphorylation sites were a substrate for
a tyrosine kinase? Did you think that a phosphatase adds a phosphate to a protein?
9-14
Blooms Level: 3. Apply

Gradable: automatic
Section: 09.01
9-15
12. You have identified a molecule, molecule X, that can bind to the ATP binding site of a
specific protein kinase, and prevent ATP binding. You are conducting a kinase assay using
this protein kinase and a known substrate of this kinase, and have set up the reaction using the
proper conditions and co-factors to allow for optimal protein kinase activity. If you add
molecule X to the reaction, what do you predict will be the outcome?
A. The substrate will be phosphorylated normally in the presence of molecule X.
B. Less phosphorylation of the substrate will be seen in the presence of molecule X.
C. More phosphorylation of the substrate will be seen in the presence of molecule X.
9-16
Clarify Question

o The question asks about the effects of a kinase inhibitor.
o You are being asked to analyze statements about the effects of a kinase inhibitor.
Gather Content
• What do you know about kinase inhibitors? What other information is related to the
question?
o The class of enzyme that adds phosphate groups from ATP to proteins is called a
protein kinase. These phosphate groups can be added to the three amino acids that have an
OH as part of their R group, namely serine, threonine, and tyrosine. We categorize protein
kinases as either serine–threonine or tyrosine kinases based on the amino acids they modify.
Most cytoplasmic protein kinases fall into the serine–threonine kinase class.
Choose Answer
answer?
o If this molecule prevents ATP binding to the kinase, this will inhibit the reaction
catalyzed by the kinase. This is because the kinase acts to transfer the terminal phosphate of
ATP onto its substrate. If binding to ATP is inhibited, then the kinase will not have a source
of phosphate nor the energy source needed to drive this endergonic reaction. In fact, this is an
approach that is used by multiple drugs that are known kinase inhibitors.
Reflect on Process
o This question asked you to analyze statements about the effects of a kinase inhibitor. If
you got the correct answer, great job! If you got an incorrect answer, where did the process
break down? Did you think that the substrate could be phosphorylated without the activity of
the kinase? Did you think that the inhibitor would increase kinase activity?

Gradable: automatic
Section: 09.01
9-17
13. Why are phosphorylation and dephosphorylation reactions commonly used to regulate
signal transduction pathways?
A. Phosphate groups are efficient second messengers
B. Protein kinases and phosphatases are abundant in most cells
C. The hydrolysis of bound GTP generates GDP, which can change the activity of proteins
bound to GDP
D. The addition or removal of a phosphate group can expose or hide potential binding sites in
proteins or change protein activity

Gradable: automatic
Section: 09.01
9-18
14. You are performing an experiment to assay phosphorylation of a substrate by a protein

kinase. Based on the data in the table below, what do these experimental results suggest?
A. GTP is not required for phosphorylation.

B. The substrate can undergo autophosphorylation.
C. The substrate is not required for phosphorylation.
D. The protein kinase is required for phosphorylation.
9-19
Clarify Question

o The question asks about the results of a phosphorylation assay.
o You are being asked to analyze the results of a phosphorylation assay.
Gather Content
• What do you know about phosphorylation? What other information is related to the
question?
o The class of enzyme that adds phosphate groups from GTP to substrates is called a
kinase. These phosphate groups can be added to the substrate by the enzyme. In the assay, a
“+” indicates that that component was added to the reaction and a “–“ indicates that it was left
out.
Choose Answer
answer?
o In the experiment the substrate was phosphorylated in the two conditions where the
substrate and GTP were present. The substrate could still be phosphorylated when the kinase
was absent, indicating that the kinase was not necessary for phosphorylation. The best answer
is that the substrate could phosphorylate itself even in the absence of the kinase.
Reflect on Process
o This question asked you to analyze the results of a phosphorylation assay. If you got
the correct answer, great job! If you got an incorrect answer, where did the process break
down? Did you think that the kinase was necessary for phosphorylation of the substrate? Did
you think that GTP was not necessary for phosphorylation of the substrate?

Gradable: automatic
Section: 09.01
9-20
15. These molecules can directly convert extracellular signals into intracellular signals.
A. Second messengers
B. Scaffolds
C. Membrane receptors
D. Adapter proteins
E. G proteins

Gradable: automatic
Section: 09.02
16. When bound to ligand, this type of receptor changes conformation to allow ions to move
down their concentration gradient across the membrane:
A. Channel-linked receptor
B. Enzymatic receptor
C. G protein-coupled receptor
D. Steroid hormone receptor

Gradable: automatic
Section: 09.02
17. Growth of new blood vessels is stimulated by vascular endothelial growth factor (VEGF).
This ligand binds to the VEGF receptor, which leads to the dimerization and
autophosphorylation of this receptor on cytoplasmic tyrosines. What type of receptor is the
VEGF receptor?

Gradable: automatic
Section: 09.02
9-21
18. What type of receptor is not an enzyme, but is directly associated with an enzyme that
can hydrolyze GTP?

Gradable: automatic
Section: 09.02
19. You are planning to perform some protein-protein interaction studies to identify a
receptor for a steroid hormone you have been working on. You start by fractionating the cell.
What cell fraction would you want to work with to identify the steroid hormone receptor of
interest?
A. The plasma membrane fraction
B. The extracellular fraction
C. The cytoplasmic fraction
D. The mitochondrial fraction
E. The ribosomal fraction
Steroid hormone receptors are intracellular receptors, and of these choices, would most likely
be found in the cytoplasm.

Gradable: automatic
LO: 09.03.01 Describe the chemical nature of ligands for intracellular receptors.
Section: 09.03
Topic: Intracellular Receptors
9-22
20. What property defines most ligands for intracellular receptors?

A. They are lipid-soluble
B. They are hydrophilic
C. They are molecules that can perform significant hydrogen bonding interactions with water
D. They are large molecules
They are mostly lipophilic molecules so that they can penetrate the lipid bilayer and interact
with their receptors.

Gradable: automatic
Section: 09.03
Type: Concept Connection
9-23
21. You are interested in developing an inhibitor for the estrogen receptor. You have
identified a molecule that is small and hydrophilic. In a test tube, this inhibitor binds tightly to
the estrogen receptor, and inhibits the interaction of the receptor with estrogen. Do you think
that this molecule will be an effective inhibitor of the estrogen receptor in cells?
A. Yes, because it can prevent estrogen binding.
B. Yes, because it is small.
C. No, because it is hydrophilic.
D. No, because it will need to bind to the DNA-binding domain to act as an inhibitor.
9-24
Clarify Question

o The question asks about an inhibitor of the estrogen receptor.
o You are being asked to analyze statements about an inhibitor of the estrogen receptor.
Gather Content
• What do you know about an inhibitor of the estrogen receptor? What other information
is related to the question?
o The nonpolar structure of steroid hormones like estrogen allows these hormones to
cross the membrane and bind to intracellular receptors. The location of steroid hormone
receptors prior to hormone binding is cytoplasmic, but their primary site of action is in the
nucleus. Binding ofthe hormone to the receptor causes the complex to shift from the
cytoplasm to the nucleus. As the ligand–receptor complex makes it all the way to the nucleus
of the cell, these receptors are often called nuclear receptors.
Choose Answer
answer?
o Because this molecule is hydrophilic, it will have a difficult time passing through the
plasma membrane. Because the estrogen receptor is an intracellular receptor, this will not
likely be an effective inhibitor. If the molecule were hydrophobic then it would be a good
inhibitor.
Reflect on Process
o This question asked you to analyze statements about an inhibitor of the estrogen
receptor. If you got the correct answer, great job! If you got an incorrect answer, where did
the process break down? Did you think that the inhibitor could diffuse across the membrane
even though it is hydrophilic? Did you think that the estrogen receptor was on the surface of
the cell?

Gradable: automatic
Section: 09.03
9-25
22. Tamoxifen is a drug that is used to treat breast cancer. It inhibits the activities of
the estrogen receptor in breast epithelial cells, which are the cells that are relevant to breast
cancer. One of the concerns that scientists had during the development of Tamoxifen as a
therapy for breast cancer was that other cell types require estrogen signaling for their function.
For example, it is known that cells in bone tissue require estrogen signaling. As a result, there
was a concern that use of Tamoxifen would lead to bone loss in patients. In reality, however,
researchers were surprised to find that Tamoxifen actually led to an increase in bone density
in breast cancer patients. At the same time, Tamoxifen did inhibit the activity of the estrogen
receptor in breast epithelial cells in these patients. What is the best explanation for this
finding?
A. Tamoxifen binds different parts of the estrogen receptor in different tissues.
B. The estrogen receptor is bound to different coactivators in different tissues.
C. Tamoxifen can only enter certain cell types.
D. Bone cells make use of a different type of estrogen receptor that does not bind to
Tamoxifen.
9-26
Clarify Question

o The question asks about the effects of tamoxifen on different cells after binding to the
estrogen receptor.
o You are being asked to evaluate explanations for the effects of tamoxifen on different
cells after binding to the estrogen receptor.
Gather Content
• What do you know about the effects of tamoxifen on different cells after binding to the
estrogen receptor? What other information is related to the question?
o The nonpolar structure of steroid hormones like estrogen allows these hormones to
cross the membrane and bind to intracellular receptors. The location of steroid hormone
receptors prior to hormone binding is cytoplasmic, but their primary site of action is in the
nucleus. Binding ofthe hormone to the receptor causes the complex to shift from the
cytoplasm to the nucleus. As the ligand–receptor complex makes it all the way to the nucleus
of the cell, where they bind to different cofactors in the nucleus. Depending on which
cofactors the estrogen receptor binds to, different genes will be turned on in different cell
types.
Choose Answer
answer?
o Tamoxifen binding in breast epithelial cells results in the recruitment of different
coactivators than are recruited when tamoxifen binds to the estrogen receptor in bone tissue.
Tamoxifen can clearly enter bone cells and bind to the estrogen receptors there, as there is an
increase in bone density in patients being treated with Tamoxifen. Reflect on Process
o This question asked you to evaluate explanations for the effects of tamoxifen on
different cells after binding to the estrogen receptor. If you got the correct answer, great job!
If you got an incorrect answer, where did the process break down? Did you think that
tamoxifen could not enter bone cells? Did you think that bone cells made a different estrogen
receptor?
Blooms Level: 5. Evaluate

Gradable: automatic
LO: 09.03.02 Diagram the pathway of signal transduction through intracellular receptors.
Section: 09.03
9-27
23. A mutation in the DNA-binding domain of a steroid hormone receptor is most likely to
affect what aspect of receptor function?
A. The conformational change of the receptor
B. The binding of the hormone to the receptor
C. The translocation of the receptor to the nucleus
D. The cellular response to the hormone
9-28
Clarify Question

o The question asks about steroid receptors.
o You are being asked to analyze statements about steroid receptors.
Gather Content
• What do you know about steroid receptors? What other information is related to the
question?
o The nonpolar structure of steroid hormones allows these hormones to cross the
membrane and bind to intracellular receptors. The location of steroid hormone receptors prior
to hormone binding is cytoplasmic, but their primary site of action is in the nucleus. Binding
ofthe hormone to the receptor causes the complex to shift from the cytoplasm to the nucleus.
In the nucleus the steroid receptor binds to DNA turning on different genes will be turned on
in different cell types.
Choose Answer
answer?
o A mutation in the DNA-binding domain of a steroid receptor would prevent it from
binding to the promoters of some genes. If these genes were not expressed normally it would
affect the cellular response to the hormone. A mutation in the DNA binding domain would
not affect the binding of the hormone to the receptor, its conformational change after binding,
or moving into the nucleus.
Reflect on Process
o This question asked you to analyze statements about steroid receptors. If you got the
correct answer, great job! If you got an incorrect answer, where did the process break down?
Did you think that mutations in the DNA binding domain of a steroid receptor would affect its
ability to bind to the hormone? Did you think that mutations in the DNA binding domain of a
steroid receptor would affect its movement to the nucleus?

Gradable: automatic
Section: 09.03
9-29
24. You are having lunch with an elderly friend when suddenly he begins to experience chest
pain and tightness. He reaches into his pocket, gets out one of his nitroglycerin tablets and
quickly takes it. After the episode passes, your friend asks you how the nitroglycerin helps his
angina. You explain that nitroglycerin gets converted by cells to nitric oxide (NO) causing the
smooth muscle cells of the blood vessel to relax and increase blood flow to the heart. He
pushes you for a more detailed explanation, so you explain further that:
A. NO activates guanylyl cyclase, which catalyzes the synthesis of cGMP, which acts as an
intracellular messenger in a pathway leading to smooth muscle relaxation.
B. NO activates a protein kinase which catalyzes the synthesis of cGMP, which acts as an
C. NO inhibits guanylyl cyclase, which allows the build up of cGMP, which acts as an
D. NO activates cGMP, which catalyzes the synthesis of guanylyl cyclase, which acts as an

Gradable: automatic
Section: 09.03
25. What is the mechanism by which binding of testosterone to the testosterone receptor
leads to upregulated gene transcription?
A. Binding of testosterone to the testosterone receptor leads to the increase in second
messengers that activate a kinase cascade, ultimately leading to the activation of transcription
factors that promote gene transcription.
B. Binding of testosterone to the testosterone receptor leads to the activation of a G protein
that stimulates the activation of enzymes that promote gene transcription.
C. Binding of testosterone to the testosterone receptor leads to a conformational change that
allows the receptor to enter the nucleus where it can bind to DNA and promote gene
transcription.
D. Binding of testosterone to the testosterone receptor leads to the opening of an ion channel
that leads to an increase in calcium in the cytoplasm. The increased calcium levels activate
calmodulin, which can go on to activate other proteins that promote gene transcription.

Gradable: automatic
Section: 09.03
9-30
26. How are receptor tyrosine kinases and steroid hormone receptors similar?
A. Both are activated by autophosphorylation
B. Both are transmembrane proteins with a single transmembrane domain
C. Both have a DNA-binding domain
D. Both have a site for binding ligand

Gradable: automatic
LO: 09.04.01 Compare the function of RTKs to steroid hormone receptors.
Section: 09.04
Topic: Signal Transduction Through Receptor Kinases
9-31
27. Some cancers are caused by the overexpression of receptor tyrosine kinases (RTKs). It is
known that RTK signaling pathways commonly stimulate cell division. Why would the
overexpression of receptor tyrosine kinases lead to cancer development?
A. RTKs are activated by dimerization, caused by ligand binding. If there are too many
receptors on the cell surface, it is possible that these receptors dimerize in the absence of
ligand binding, thus stimulating cell division at inappropriate times.
B. If there are too many RTKs on the cell surface, this will tend to allow cells to adhere to
each other. Once they adhere, RTKs from one cell can bind to RTKs from another cell, and
they can activate each other leading to activation of downstream signaling pathways in both
cells.
C. If there are too many RTKs on the cell surface, it is less likely that inhibitors will bind to
all of the available RTKs and block their ability to enter the nucleus. As a result, some of the
RTKs will be able to enter the nucleus to stimulate transcription.
D. If there are too many RTKs on the cell surface, this will promote the inhibition of
autophosphorylation. In the absence of autophosphorylation, it is more likely that the RTK
downstream signaling pathway will be active.
9-32
Clarify Question

o The question asks about over expression of receptor tyrosine kinases.
o You are being asked to analyze statements about over expression of receptor tyrosine
kinases.
Gather Content
• What do you know about receptor tyrosine kinases? What other information is related to
the question?
o Receptor tyrosine kinases have a relatively simple structure consisting of a single
transmembrane domain, an extracellular ligand-binding domain, and an intracellular kinase
domain. This kinase domain contains the catalytic site of the receptor, which acts as a protein
kinase that adds phosphate groups to tyrosines. On ligand binding to a specific receptor, two
of these receptor–ligand dimerize and phosphorylate each other,.
Choose Answer
answer?
o Dimerization leads to activation of RTKs, and thus if there are too many receptors on
the cell surface, it is more likely that dimerization and activation of the signaling pathway will
happen in the absence of ligand. This can lead to the inappropriate activation of a signaling
pathway that promotes cell division. Dimerization and autophosphorylation has to occur with
RTKs in the same cell. There is no mechanism for this occurring between two different cells.
RTKs are membrane bound proteins that do not enter the nucleus. Autophosphorylation is
necessary for activation of this pathway and thus if autophosphorylation were inhibited, it
would be less likely that the downstream pathway would be active.
Reflect on Process
o This question asked you to analyze statements about over expression of receptor
tyrosine kinases. If you got the correct answer, great job! If you got an incorrect answer,
where did the process break down? Did you think that receptor tyrosine kinases allow cells to
bind to each other? Did you think that receptor tyrosine kinases enter the nucleus of a cell
once they are activated?
9-33

Gradable: automatic
Section: 09.04
28. What signaling pathway commonly makes use of a G protein to transduce the signal?
A. Channel-linked receptor pathways
B. Steroid hormone receptor pathways
C. Receptor tyrosine kinase pathways
Receptor tyrosine kinase pathways commonly use the protein Ras to transduce the signal. Ras
is a small G protein.

Gradable: automatic
Section: 09.04
9-34
29. Your research project involves the characterization of a particular signal transduction
pathway. Specifically, you have been studying a receptor tyrosine kinase and protein X,
which initiates downstream events. You are certain that protein X is part of the signal
transduction pathway, but have been unable to identify a direct protein-protein interaction
between the receptor tyrosine kinase and the protein X. What should you do next in your
attempt to identify a link between the receptor tyrosine kinase and protein X?
A. Try to identify a coactivator protein.
B. Try to identify proteins that act downstream of protein X.
C. Try to identify an adapter protein that can interact with both the receptor and protein X.
D. Confirm the interaction between the receptor tyrosine kinase and its ligand.
9-35
Clarify Question

o The question asks about the signaling pathway activated by a receptor tyrosine kinase.
o You are being asked to evaluate an experiment on the signaling pathway activated by
a receptor tyrosine kinase.
Gather Content
• What do you know about the signaling pathway activated by a receptor tyrosine kinase?
What other information is related to the question?
o When a receptor tyrosine kinase is activated it dimerizes and autophosphorylates
itself. This then passes a signal to adapter proteins that carry the signal to other proteins in the
cell. At the end of the signaling pathway a transcription factor is typically activated increasing
gene expression.
Choose Answer
answer?
o If the receptor and protein X do not seem to be interacting directly then it is possible
that another adapter protein is necessary to carry the signal from the receptor to protein X.
Reflect on Process
o This question asked you to evaluate an experiment on the signaling pathway activated
by a receptor tyrosine kinase. If you got the correct answer, great job! If you got an incorrect
answer, where did the process break down? Did you think that proteins downstream of protein
X would affect the interaction between the receptor and protein X? Did you think that the
interaction between the ligand and receptor would interfere with binding between the receptor
and protein X?
Blooms Level: 5. Evaluate

Gradable: automatic
LO: 09.04.02 Describe how information crosses the membrane in RTKs.
Section: 09.04
9-36
30. The protein SOS is a guanine nucleotide exchange factor for Ras. SOS helps facilitate the
exchange of GDP for GTP. What would be the effect of a mutation that inhibits the
interaction between SOS and Ras?
A. GTP would remain bound to Ras, thereby keeping Ras constitutively active.
B. GDP would remain bound to Ras, thereby preventing Ras activation.
C. Ras would be more likely to hydrolyze GTP to GDP.
D. There would be no effect.
Clarify Question

o The question asks about the interaction between Ras and SOS.
o You are being asked to analyze what would happen if Ras and SOS could not interact.
Gather Content
• What do you know about the interaction between Ras and SOS? What other information
is related to the question?
o The protein SOS is a guanine nucleotide exchange factor for Ras. SOS helps facilitate
the exchange of GDP for GTP.Ras is a G-protein that is active when GTP is bound to it. Ras
can then cleave a phosphate off of GTP forming GDP to go into the inactive state. When SOS
replaces GDP with GTP it reactivates the Ras.
Choose Answer
answer?
o Without SOS, Ras would have GDP bound to it and could not replace the GDP with
GTP. Without GTP, the Ras would be inactive.
Reflect on Process
o This question asked you to analyze what would happen if Ras and SOS could not
interact. If you got the correct answer, great job! If you got an incorrect answer, where did the
process break down? Did you think that GTP would remain bound to Ras in the absence of
SOS? Did you think that Ras would increase breakdown of GTP into GDP?
9-37

Gradable: automatic
Section: 09.04
31. Many receptor tyrosine kinase (RTK) pathways lead to the activation of Ras. To activate
Ras, it is necessary to recruit a guanine nucleotide exchange factor to the plasma membrane,
because Ras is a membrane associated protein. Guanine nucleotide exchange factors, such as
SOS, stimulate the exchange of GDP for GTP. However, SOS cannot bind directly to most
RTKs. The protein Grb2 has a domain that can bind to phosphorylated tyrosines, and another
domain that can bind to SOS. Therefore, Grb2 can bind to active RTKs and recruit SOS to the
plasma membrane. Grb2 is an example of what kind of signaling molecule?
A. Scaffold
B. Adapter protein
C. Second messenger
D. Enzyme

Gradable: automatic
Section: 09.04
32. Ste5 binds to MAPKKK, MAPKK, and MAPK to organize the kinase cascade. What type
of signaling molecule is Ste5?
A. Scaffold
B. Adapter protein
C. Second messenger
D. Enzyme

Gradable: automatic
Section: 09.04
9-38
33. Many receptor tyrosine kinase pathways have MAPK as a downstream signaling
component. MAPK can phosphorylate target proteins. What type of signaling molecule is
MAPK?
A. Scaffold
B. Adapter protein
C. Second messenger
D. Enzyme

Gradable: automatic
Section: 09.04
34.
A small number of cell surface receptors can ultimately generate a large intracellular response due to activation of kinase
cascades. This is referred to as:
A. signal amplification.
B. signal transduction.
C. signal dampening.
D. signal activation.

Gradable: automatic
LO: 09.04.03 Explain the role of kinase cascades in signal transduction.
Section: 09.04
35. What enzyme phosphorylates MAP kinase kinase?

A. MAP kinase
B. MAP kinase kinase
C. MAP kinase kinase kinase
D. MAP phosphatase

Gradable: automatic
LO: 09.04.03 Explain the role of kinase cascades in signal transduction.
Section: 09.04
9-39
36. The cell surface receptors that can act only indirectly on plasma membrane-bound
enzymes or ion channels are called:
A. G protein-coupled receptors.
B. gated ion channels.
C. enzymatic receptors.
D. second messenger receptors.

Gradable: automatic
LO: 09.05.01 Contrast signaling through GPCRs and RTKs.
Section: 09.05
Topic: Signal Transduction Through G Protein-Coupled Receptors
37. G protein-coupled receptors are the largest family of cell surface receptors. Each receptor
passes through the plasma membrane how many times?
A. Once
B. Three times
C. Five times
D. Seven times

Gradable: automatic
Section: 09.05
38. In the nitric oxide signaling pathway, nitric oxide activates an enzyme that can convert
many molecules of GTP into molecules of cGMP. cGMP is a small molecule that can diffuse
through the cytoplasm and bind to an enzyme called protein kinase G (PKG). Binding of
cGMP to PKG leads to a change in the confirmation of PKG that leads to its activation. What
type of signaling molecule is cGMP?
A. Scaffold
B. Adapter protein
C. Second messenger
D. Enzyme

Gradable: automatic
LO: 09.05.02 Relate the function of second messengers to signal transduction pathways.
Section: 09.05
9-40
39. Some enzymatic receptors and most G protein-coupled receptors transmit the signal into
the cytoplasm by utilizing other substances within the cytoplasm that are referred to as:
A. genes.
B. intracellular receptors.
C. second messengers.
D. first messengers.

Gradable: automatic
Section: 09.05
40. A mutation that affects Ca++ binding to calmodulin is most likely to interfere with what
aspect of a signal transduction pathway?
A. The flow of Ca++ ions through ion channel receptors
B. The cellular response to the second messenger
C. The MAP kinase cascade
D. G protein activity

Gradable: automatic
Section: 09.05
9-41
41. If the effector protein phospholipase C failed to cleave phosphatidylinositol-4,5-

bisphosphate (PIP2), the action of what enzyme would be affected?
A. cAMP
B. IP3
C. protein kinase A (PKA)
D. protein kinase C (PKC)
9-42
Clarify Question

o The question asks about enzymes activated by inositol triphosphate.
o You are being asked to apply your knowledge aboutenzymes activated by inositol
triphosphate.
Gather Content
• What do you know about enzymes activated by inositol triphosphate? What other
information is related to the question?
o A common second messenger is produced from the molecules called inositol
phospholipids. These are inserted into the plasma membrane by their lipid ends and have the
inositol phosphate portion protruding into the cytoplasm. The most common inositol
phospholipid is phosphatidylinositol-4,5-bisphosphate (PIP2). This molecule is a substrate of
the effector protein phospholipase C, which cleaves PIP2 to yield diacylglycerol (DAG) and
inositol-1,4,5-trisphosphate (IP3).Both of these compounds then act as second messengers
with a variety of cellular effects. DAG, like cAMP, can activate a protein kinase, in this case
protein kinase C (PKC).
Choose Answer
answer?
o When inositol triphosphate (IP3) is produced by phospholipase C it actives protein
kinase C. Protein kinase A is activated by cAMP. cAMP and IP3 are second messengers and
not enzymes.
Reflect on Process
o This question asked you to apply your knowledge about enzymes activated by inositol
triphosphate. If you got the correct answer, great job! If you got an incorrect answer, where
did the process break down? Did you think thatcAMPor IP3were enzymes? Did you think that
protein kinase A was activated by IP3?

Gradable: automatic
Section: 09.05
9-43
42. What is similar about G protein-coupled receptors (GPCRs) and receptor tyrosine kinases
(RTKs)?
A. Both are directly bound to G proteins
B. Both can activate phospholipase C
C. Both are enzymes
D. Both are activated by autophosphorylation

Gradable: automatic
Section: 09.05
43. The function of adenylyl cyclase is to:

A. catalyze the conversion of ATP to cAMP.
B. cleave PIP2 into DAG and IP3.
C. directly activate protein kinase A (PKA).
D. stimulate the release of calcium from the endoplasmic reticulum.

Gradable: automatic
Section: 09.05
44. What is the difference between Ras and the G proteins bound to G protein coupled
receptors (GPCRs)?
A. Ras is an enzyme and the G proteins bound to GPCRs are not enzymes.
B. Ras is a second messenger and the G proteins bound to GPCRs are not second messengers.
C. Ras is a small G protein and the G proteins bound to GPCRs are not small G proteins.
D. Ras can activate different effector molecules and the G proteins bound to GPCRs cannot
activate different effector molecules.

Gradable: automatic
Section: 09.05
9-44
45. What second messenger is directly involved in activating protein kinase C (PKC)?
A. DAG
B. cAMP
C. cGMP
D. Phospholipase C
E. G protein

Gradable: automatic
Section: 09.05
9-45

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Chapter 09 - Cell Communication

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Multiple Choice Questions

Blooms Level: 2. Understand

Blooms Level: 1. Remember

3. In synaptic signaling, neurotransmitters are released into a space that is referred to as a:

Blooms Level: 1. Remember

Blooms Level: 2. Understand

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

• What is the key concept addressed by the question?

Blooms Level: 3. Apply

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 2. Understand

9. Addison's disease is a disorder that results from a reduction in production of

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

10. What is the function of a protein kinase?

Protein kinases phosphorylate proteins

Blooms Level: 1. Remember

• What is the key concept addressed by the question?

• What do you know about phosphorylation of a protein? What other information is

Blooms Level: 3. Apply

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 2. Understand

14. You are performing an experiment to assay phosphorylation of a substrate by a protein

A. GTP is not required for phosphorylation.

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 2. Understand

Blooms Level: 2. Understand

Blooms Level: 2. Understand

20. What property defines most ligands for intracellular receptors?

Blooms Level: 2. Understand

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

• What is the key concept addressed by the question?

Blooms Level: 5. Evaluate

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 2. Understand

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 2. Understand

• What is the key concept addressed by the question?

Blooms Level: 5. Evaluate

• What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 1. Remember