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Essential Cell Biology 5th edition

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Questions

571

KEY TERMS

adaptation GTP-binding protein phosphoinositide 3-kinase

adenylyl cyclase hormone (PI 3-kinase)

Ca 2+ /calmodulin-dependent inositol 1,4,5-trisphosphate phospholipase C

protein kinase (CaM-kinase) (IP 3 ) protein kinase

calmodulin inositol phospholipid protein kinase C (PKC)

cell signaling intracellular signaling pathway protein phosphatase

cyclic AMP ion-channel-coupled receptor Ras

cyclic-AMP-dependent local mediator receptor

protein kinase (PKA) MAP kinase receptor serine/threonine kinase

diacylglycerol (DAG) MAP-kinase signaling module receptor tyrosine kinase (RTK)

enzyme-coupled receptor molecular switch serine/threonine kinase

extracellular signal molecule monomeric GTPase signal transduction

G protein neurotransmitter steroid hormone

G-protein-coupled receptor nitric oxide (NO) tyrosine kinase

(GPCR)

nuclear receptor

QUESTIONS

QUESTION 16–8

Which of the following statements are correct? Explain your

answers.

A. The extracellular signal molecule acetylcholine has

different effects on different cell types in an animal and

often binds to different cell-surface receptor molecules on

different cell types.

B. After acetylcholine is secreted from cells, it is long-lived,

because it has to reach target cells all over the body.

C. Both the GTP-bound α subunits and nucleotide-free

βγ complexes—but not GDP-bound, fully assembled

G proteins—can activate other molecules downstream of

GPCRs.

D. IP 3 is produced directly by cleavage of an inositol

phospholipid without incorporation of an additional

phosphate group.

E. Calmodulin regulates the intracellular Ca 2+

concentration.

F. Different signals originating from the plasma membrane

can be integrated by cross-talk between different signaling

pathways inside the cell.

G. Tyrosine phosphorylation serves to build binding sites

for other proteins to bind to RTKs.

QUESTION 16–9

The Ras protein functions as a molecular switch that is set

to its “on” state by other proteins that cause it to release

its bound GDP and bind GTP. A GTPase-activating protein

helps reset the switch to the “off” state by inducing Ras

to hydrolyze its bound GTP to GDP much more rapidly

than it would without this encouragement. Thus, Ras works

like a light switch that one person turns on and another

turns off. You are studying a mutant cell that lacks the

GTPase-activating protein. What abnormalities would you

expect to find in the way in which Ras activity responds to

extracellular signals?

QUESTION 16–10

A. Compare and contrast signaling by neurons, which

secrete neurotransmitters at synapses, with signaling carried

out by endocrine cells, which secrete hormones into the

blood.

B. Discuss the relative advantages of the two mechanisms.

QUESTION 16–11

Two intracellular molecules, X and Y, are both normally

synthesized at a constant rate of 1000 molecules per second

per cell. Molecule X is broken down slowly: each molecule

of X survives on average for 100 seconds. Molecule Y is

broken down 10 times faster: each molecule of Y survives

on average for 10 seconds.

A. Calculate how many molecules of X and Y the cell

contains at any time.

B. If the rates of synthesis of both X and Y are suddenly

increased tenfold to 10,000 molecules per second per cell—

without any change in their degradation rates—how many

molecules of X and Y will there be after one second?

C. Which molecule would be preferred for rapid signaling?

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