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- Phosphorylase kinase integrates signals from thecyclic-AMP-dependent and Ca2+-dependent signalingpathways that control glycogen breakdown in liver andmuscle cells (Figure Q15–4). Phosphorylase kinase is com-posed of four subunits. One is the protein kinase that cata-lyzes the addition of phosphate to glycogen phosphorylaseto activate it for glycogen breakdown. The other three sub-units are regulatory proteins that control the activity of thecatalytic subunit. Two contain sites for phosphorylation byPKA, which is activated by cyclic AMP. The remaining sub-unit is calmodulin, which binds Ca2+ when the cytosolicCa2+ concentration rises. The regulatory subunits controlthe equilibrium between the active and inactive confor-mations of the catalytic subunit, with each phosphate andCa2+ nudging the equilibrium toward the active confor-mation. How does this arrangement allow phosphorylasekinase to serve its role as an integrator protein for the mul-tiple pathways that stimulate glycogen…Choices for each phrases: a, b, y, t, v, e; gtp, cgt, atp, adp, camp, catp; gtp, gdp, atp, adp, camp, catp; histamine kinase, gaunylyl cyclamen, phosphorylation, adenylyl cyclaseMatching :1. MDR protein Part of NAD molecule ______ 2. SGLT Part of FAD molecule _____ 3. Grb-2 Raises intestinal pH _______ 4. Cholecystokinin Oxidizes C-C bonds ___________ 5. Chylomicron Has higher phosphoryl transfer potential than ATP __ 6. Secretin An ABC transporter ______ 7. Niacin Sodium-glucose symporter ______ 8. Flavin Lipoprotein complex ______ 9. FAD Found in EGF pathway _____ Phosphoenolpyruvate Signals release of digestive enzymes
- How does PKC’s signaling role change in response to growth factor signaling versus an immune response? PKC interacts directly with signaling molecules in both cascades, but only exhibits kinase activity during growth factor signaling. PKC interacts directly with signaling molecules in growth factor cascades, but interacts with signaling inhibitors during immune signaling. PKC amplifies growth factor cascades, but turns off immune cascades. PKC is activated during growth factor cascades, but is inactivated during immune response cascades.A scientist notices that a cancer cell line shows high levels of phosphorylated ERK in the absence of EGF. What are two possible explanations for the increase in phosphorylated ERK? Be specific in which proteins are involved.Autophagy Is Required for PKA Activation and Cell Viability upon GlucoseStarvation. The functional relationship between PKA and autophagyis largely unclear. Because PKA controls cell metabolism particularly related to glucose status (21–23), we first examined the relationship between autophagy and PKA activity in the control of cellmetabolism with glucose limitation. We found that in addition toactivating autophagy, glucose starvation also induced the phosphorylation of cAMP response element-binding (p-CREB), a wellknown PKA substrate, indicative of elevated PKA activity in bothHEK293T and HCT116 cells. In contrast, disruption of autophagyby deletion of essential autophagy gene Atg7 or Atg14 abolished theincrease of p-CREB levels in the above cells (SI Appendix, Fig.S1 A, B, D, and E), suggesting that inactivation of autophagy suppresses PKA activity in response to energy shortage. Moreover, lossof Atg7 or Atg14 accelerated cell death in response to glucosestarvation (SI Appendix, Fig.…
- 2. The Ca2+ ATPase pumps on the sarcoplasmic reticulum membrane play an important role in muscle contraction. In patients with muscular dystrophy, there is some evidence that shows the expression of the Ca2+ ATPase pumps is diminished (there are fewer). Which of the following cellular effects may be a result of the diminished number of Ca2+ ATPase pumps? A)Reduced Ca2+ release through the RyR B)Reduced Ca2+ uptake into the SR C)Slowed activity of the Na/K pump D)Reduced communication between the DHP receptor and the Ca2+ ATPase pumps E)Reduced communication between the DHP Receptor and the Ryanodine receptorQ28. An ABC transporter consists of two domains: the transmembrane domain (shown here as Y) and the ATP-binding cassette domain (shown here as Z). Which of the following statements correctly identifies a difference between these two domains? The hydropathy index is higher for Y than Z. Exchanging domain Y with domain Z would not affect the function. Exchanging domain Z with the same domain from a different ABC transporter will not alter the specificity of transport, but swapping Y domains will. Alpha helices are only found in the Y domain. A. 1,2 and 3 B. 1 and 3 C. 2 and 4 D. 4 only E. All of 1,2,3 and 4 are correct14. How did they do that? A strain of mice has been developed that lack the enzyme phosphorylase kinase. Yet, after strenuous exercise, the glycogen stores of a mouse of this strain are depleted. Explain how this depletion is possible.
- EGF-R patho Discuss how the EGF-R becomes activeo How does the active receptor recruit substrate, and how does substrate hold ontoreceptor? When held, what “options” in regards to what the receptor does tobound substrate?o What proteins are involved in the recruitment of ras to the receptor, and how doesras become active – what does it do then? Make sure you include the G-proteinstory.o When active, ras triggers the MAPK cascade – what is the end result of this path.o Discuss the most common mutation in the ras gene found in cancer cells – how doesthis mutation play a role in the cancer cell story?6)During the epinephrine signaling pathway we learned about in class, the enzyme glycogen phosphorylase is regulated by: Zymogen activation Competitive inhibition Allosteric regulation Covalent modificationWhat is the function of a phosphatase? A phosphatase removes phosphorylated amino acids from proteins. A phosphatase removes the phosphate group from phosphorylated amino acid residues in a protein. A phosphatase phosphorylates serine, threonine, and tyrosine residues. A phosphatase degrades second messengers in the cell.
