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- See figure 12.16b regarding the process by which cyclin regulates the Cdk. Suppose that the cyclin binding site in the Cdk contains these FOUR amino acids in this order from top to bottom: serine, lysine, aspartic acid acid and lysine and the Cdk binding site in the cyclin contains these FOUR amino acids in this order from top to bottom: aspartic acid, aspartic acid, lysine and serine. Use the schematics below to show the R groups and how they might interact to create the cyclin.cdk complex. Label both binding sites, show all charges that will be used to create any bonds, and label all bonds formed and add the ATP active site. A Explain what a kinase does and how the cyclin controls the activity of the Cdk.TGF-B Receptor I (RI) phosphorylation of Smad2/3 does all of the following EXCEPT: activate Smad2/3 binding to the Co-Smad Smad4 dissociate intramolecular binding of Smad2/3 MH1 and MH2 domains. RI phosphorylation of Smad2/3 does all of these things. release Smad2/3 from the nucleus into the cytoplasm unmask the Smad2/3 nuclear localization signal (NLS).Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.
- Please use Transferrin receptor as an example of the protein whose pathway is being traced. If it is easier or possible, can there be a labeled drawing to explain.Autophagy is an évolutionary conserved catabolic process devoted to the degradation of intracellular components. Which of the following would you observe during autophagy? Select all that apply MTOR inhibition through phosphorylation and activation of TSC proteins MTOR activation and phosphorylation of downstream target proteins Increased expression of Rab7 which mediates lysosomal fusion Acute inflammatory responseNucleation of straight, single line microfilaments is mediated by which of the following? Rho GTPase and Formin Rho GTPase and Arp 2/3 Cdc42 GTPase and Arp2/3 OCdc42 GTPase and Formin 14 < Previous
- If you wanted to engineer the initiator caspase from the Fas/FasL extrinsic apoptosis pathway to function in the intrinsic pathway (e.g. in response to DNA damage), which of the following would be the most likely approach to succeed? O Replace the extrinsic pathway's initiator caspase Death Effector Domain with a CARD domain O Replace the Fas Death Domain with a cytochrome C binding domain O Generate a version of the Fas receptor that localizes to the mitochondrial intermembrane space 80 O Replace the intrinsic pathway's initiator caspase CARD domain with a Death Effector Domain F3 0 $ 4 DOD DOO R F4 S % 5 T No new data to save. Last checked at 3:01pm Submit Qu B4 ♫ 8 tv A F5 < 6 MacBook Air F6 Y & 7 F7 * 8 X F8 ( 9You have isolated a new species of infectious bacteria. The bacterium releases a toxin that you believe is adversely affecting heterotrimeric Gs (stimulatory)-protein-based signaling. To explore this hypothesis you use an epithelial cell line that is expressing a cyan fluorescent protein (CFP)-labeled α subunit and a yellow fluorescent protein (YFP)-labeled β subunit of a heterotrimeric Gs-protein. CFP emits blue light and has excitation and emission wavelengths of 440 nm and 490 nm, respectively. YFP emits yellow light and has excitation and emission wavelengths of 490 nm and 527 nm, respectively. To test your hypothesis, you perform two experiments. First, you apply a signaling ligand known to activate this Gs protein and track yellow fluorescence. Second, you apply the signaling ligand and the purified bacterial toxin simultaneously and track yellow fluorescence. Which of the following conclusion will you draw based on the above experimental data? The toxin locks the α subunit…The affinity of integrins for matrix components canbe modulated by changes to their cytoplasmic domains:a process known as inside-out signaling. You have iden-tified a key region in the cytoplasmic domains of αIIbβ3integrin that seems to be required for inside-out signaling(Figure Q19–3). Substitution of alanine for either D723in the β chain or R995 in the α chain leads to a high levelof spontaneous activation, under conditions where thewild-type chains are inactive. Your advisor suggests thatyou convert the aspartate in the β chain to an arginine(D723R) and the arginine in the α chain to an aspartate(R995D). You compare all three α chains (R995, R995A,and R995D) against all three β chains (D723, D723A, andD723R). You find that all pairs have a high level of sponta-neous activation, except D723 vs R995 (the wild type) andD723R vs R995D, which have low levels. Based on theseresults, how do you think the αIIbβ3 integrin is held in itsinactive state?
- Explain how CDK activity is modulated by the following proteins: (a) cyclin, (b) CAK, (c) Wee1, (d) p21.The ras protein is a mutated G protein that lacks GTPase activity. How does the absence of this activity affect the adenylyl cyclase pathway?Atherosclerosis can obstruct or block flow in arteries, including those that provide oxygenated blood to the heart. Elevated levels of [ Select ] ["LDL, and VLDL", "HDL"] are associated with atherosclerosis, most likely because of their role in delivery of lipids to peripheral tissues and cells. Smooth muscle cells are recruited to the site of damage, where they [ Select ] ["induce apoptosis of endothelial cells", "proliferate"] , hence expanding the extent of the lesion.