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aquamarinecheetah178Lv1

28 Sep 2019

A drug inhibits the ability of the glucocorticoid receptor to dimerize. How would this drug specifically affect each of the following events? Please go into detail

A. The ability of the glucocorticoid receptor to travel into the nucleus?

B. The ability of the glucocorticoid receptor to bind to GREs

C. The ability of the glucocorticoid receptor to stimulate transcription

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Hubert KochLv2

28 Sep 2019

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The EGF-receptor is a receptor tyrosine kinase that binds toepidermal growth factor (EGF). In response to EGF binding, theEGF-receptor stimulates a signaling pathway that involves Ras.Ultimately, this signaling pathway leads to the upregulation offactors that promote cell division. As a result, in response toEGF, cells that express the EGF-receptor undergo cell division toproduce more cells. If an inhibitor that inhibited all G proteinswas added to cells, how would this affect the ability of thesecells to respond to EGF?

1)The inhibitor would have no effect, because the EGF-receptoris not a G protein-coupled receptor.

2)While the receptor would dimerize and autophosphorylate in thepresence of the inhibitor, downstream signaling would be preventedbecause the inhibitor would affect Ras activity.

3)In the presence of the inhibitor, the receptor could bind toEGF and dimerize, but it would not be able to autophosphorylatebecause this requires the activity of a G protein.

amethystantelope937

1.A researcher alters the DNA-binding domain of a glucocorticoid receptor to that of an estrogen receptor. How would the cells respond to exposure to glucocorticoids?

a. They would bind estrogen, and initiate estrogen-dependent synthesis

b. They would bind glucocorticoids, and initiate testosterone-dependent synthesis

c. They would bind estrogen, and initiate testosterone-dependent synthesis

d. They would bind glucocorticoids, and initiate estrogen-dependent synthesis

e. They would bind neither hormone

2. All of the following statements about mitochondria are valid except:

a. The outer membrane of the mitochondrion is more like a eukaryotic cell plasma membrane.

b. The outer membrane of the mitochondrion is more like a prokaryotic outer membrane.

c. Mitochondria have ribosomes that are a different size from those in the rest of the cell.

d. Mitochondria have their own DNA that encodes very few proteins.

e. Mitochondria store Calcium ions

3.The unique length-tension relationship of muscle is due to:

a. the limit on the amount of ATP the muscle can produce.

b. the fact that tension is proportional to the amount of overlap between actin fibers and myosin heads

. c. the ability of kinesin to move along filaments.

d. the limit imposed on cross-sectional area of muscle in organisms.

e. the shortening of actin filaments.

4.The enzyme âFlippaseâ causes the flip-flop of dolichol phosphate from one side of a membrane to the other as part of the process leading to:

a. binding of a receptor by a ligand

b. glycosylation of newly synthesized proteins

c. transfer of proteins to the golgi apparatus.

d. membrane fusion during secretion

e. formation of coated vesicles

5. What do the photosystems of a chloroplast capture from the splitting of water during the light reactions?

a. ATP

b. Protons

c. electrons

d. neutrons

e. oxygen

The binding of platelet derived growth factor (PDGF) to the PDGF receptor stimulates phosphorylation of 8 tyrosines in the receptor's cytoplasmic domain. The enzyme phosphatidylinositol 3'kinase (PI 3-kinase) binds to one or more of the phophotyrosines through its SH2 domains and is thereby activated. To identify the activation phosphotyrosines, you synthesize 8 pentapetides that contain the critical tyrosines (at the N-terninus) in their phosphorylated or unphosphorylated forms. You then mix an excess of each of the various pentapeptides with phosphorylated PDGF receptor and PI 3-kinase. Immunoprecipitation of the PDGF receptor will bring down any bound PI 3-kinase, which can be assayed by its ability to add 32P-phosphate to its substrate.

A) Draw a flow diagram showing how this assay works.

B) Do your results support the notion that PI-kinase binds to phosphotyrosines in the activated PDGF receptor? Why or why not?

C) THe amino acid sequences of the PDGF receptor pentapeptide tested above (number accodingly to the position of tyrosine in the PDGF receptor) and peptide segments that are known to bind to PI 3-kinase in other activated receptors are shown below. Which amino acid residues are most important and why?

684 YSNAL YMMMR (FGF receptor)

708 YMDMS YTHMN (insulin receptor)

719 YVPML YEVML (hepatocyte growth factor receptor)

731 YADIE YMDMK (steel factor receptor)

739 YMAPY YVEMR (CSF-1 receptor)

743 YDNYE

746 YEPSA

755 YRATL