Hydrophobic extracellular signaling molecules would most likely interact with __
ID: 32856 • Letter: H
Question
Hydrophobic extracellular signaling molecules would most likely interact with ____________ in/on target cells.
A.
receptor tyrosine kinases
B.
intracellular receptors
C.
G protein-coupled receptors
D.
ligand-gated ion channels
E.
membrane transport proteins
0.5 points
Question 2
__________ signal(s) through enzyme-linked receptors where the receptor is not itself a kinase but instead recruits cytosolic kinases.
A.
Cytokines
B.
Insulin
C.
Adrenaline
D.
Neurotransmitters
E.
Thyroid hormones
0.5 points
Question 3
Which of the following is a post-translational modification that's oftentimes used to regulate protein function within intracellular signaling cascades?
A.
Allosteric interaction
B.
Compartmentalization
C.
Second messenger system
D.
Assembly of protein complexes
E.
Ubiquitination
0.5 points
Question 4
___________ is a common type of "allosteric switch" protein which gets directly activated by intracellular calcium.
A.
GTP-binding protein
B.
Kinase
C.
Calmodulin
D.
Phosphatase
E.
Heterotrimeric G protein
0.5 points
Question 5
When a small GTP-binding protein (GBP) is in the "on" (active) state (select any/all answers that apply):
A.
its Switch I and Switch II domains tilt toward one another.
B.
the GBP can physically interact with downstream effector molecules.
C.
GDP is bound within the nucleotide-binding pocket of the GBP.
D.
the GBP is incapable of hydrolyzing its bound GTP.
E.
the Switch II domain is phosphorylated on multiple tyrosine residues.
A.
receptor tyrosine kinases
B.
intracellular receptors
C.
G protein-coupled receptors
D.
ligand-gated ion channels
E.
membrane transport proteins
Explanation / Answer
1)
Hydrophobic extracellular signaling molecules would most likely interact with intracellular receptors. Steroid hormones are example of these.
Option B is correct.
2)
Insulin is a signal mlecule and it is phosphorylyzed through enzyme-linked receptors where the receptor is not itself a kinase but instead recruits cytosolic kinases.
Option B is correct.
3)
The post-translational modification that's oftentimes used to regulate protein function within intracellular signaling cascades is the allosteric interaction. The proteins undergo confirmational changes to get stability and to initiate the perfect binding between the ligand and receptor to trigger the signal cascade.
Option A is correct.
4)
Calmodulin is a common type of "allosteric switch" protein which gets directly activated by intracellular calcium.
Option C is correct.
5)
When a small GTP-binding protein (GBP) is in the "on" (active) state , its Switch I and Switch II domains tilt toward one another. the GBP can physically interact with downstream effector molecules. the Switch II domain is phosphorylated on multiple tyrosine residues.
Options A, B and E are correct.
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