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- Cytokine receptors and tyrosine kinase receptors are similar in all of the following ways EXCEPT one. Which one is the exception? O They are both down-regulated by lysosomal degradation They both involve receptor exoplasmic domain dimerization They both result in an effector protein entering the nucleus O They both involve cytosolic domain phosphorylationTGF-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).Select all the true statements about cyclins: (select all that applies) Group of answer choices They have functionally important regions called cyclin boxes that show high levels of homology They contain a cyclin destruction box with a conserved consensus sequence of RXXLXXIXD/N They regulate the activity of cyclin-dependent kinases (Cdks) by promoting phosphorylation of a single Thr side chain They bind protein partners with high specificity in regions called cyclin boxes..
- Cyclin-dependent kinases are a type of "microchip" protein that require multiple inputs (i.e., structural alterations) to be activated-- and thus are active only under specific conditions (as shown in the diagram below). How does limiting activity to when all conditions have been met help the cell function properly? INPUTS has this phosphate been removed? been added? has this is cyclin present? phosphateWhich of the following is false about cyclin-cdk complexes? OCdk's do not have to bind to cyclin proteins for complex to be active. OCdk/cyclin complexes phosphorylates proteins required to trigger next cell cycle phase. Process acts as molecular brakes to ensure cell is ready to continue with cell cycle. O Cyclin concentrations increase gradually, but cdk must be phosphorylated by specific kinase for complex to be activeThe destruction of the various cyclins is commonly used to inactivate the Cdk/cyclin complexes. Why is it advantageous to inactivate these complexes via protein destruction instead of some other method that does not require the re-synthesis of a cyclin protein the next time the cell divides?
- You have discovered two new inhibitors that inhibit enzymes involved in the pathway shown below. Both inhibitors are newly identified proteins. You know that one of these proteins is a noncompetitive inhibitor of the G1/S-cyclin dependent kinase (G1/S-Cdk). Another protein is a competitive inhibitor of the phosphatase (ie. a regulatory enzyme) that removes phosphates from phosphorylated Rb. mitogen activated mitogen receptor intracellular signaling pathway activated G,-Cdk and G,/S-čdk inactivated Rb protein active Rb protein inactivated transcription regulator active transcription regulator PHOSPHORYLATION OF Rb TRANSCRIPTION TRANSLATION CELL PROLIFERATION 1. What effect would the noncompetitive inhibitor of the G1/S-Cdk complex have on the Rb protein in the pathway shown above? And what effect would that have on the final outcome for these cells? 2. What effect would the competitive inhibitor of the phosphatase that acts on phosphorylated Rb have on the final outcome for these cells?…Why doesn't Cdk1 active immediately upon binding to cyclin B? What other components of the cell’s regulatory machinery could explain the delay in activation of the kinase activity?What would most likely occur to nuclear-cytoplasmic shuttling if the intrinsic GTPase activity of RAN was slowed down by 50%? Group of answer choices RAN would not bind exportin and proteins would accumulate in the nucleus All of the answers are likely None of the answers are likely Importin beta would not release from RAN in the cytoplasm and nuclear import would slow down RAN would not bind to importin beta and protein cargo in the nucleus would not release
- Which of the following would inhibit the ability of a cyclin-Cdk complex from phosphorylation target proteins? phosphorylation by Wee1 phosphorylation by CAK Cdk inhibitor protein binding A & C all of the aboveRAS is a signal transducer that acts as a switch for turning on cell division. Drag the descriptions below to their proper places on the figure to show the sequence of events. When growth factor binds to the receptor, the intracellular domain activates RAS by facilitating exchange of GDP for GTP. When no growth factor is bound to the extracellular receptor, RAS is bound to GDP and is inactive. RAS activates the first of three sequential kinase proteins termed the MAP kinase cascade. Cell proliferation proceeds as the machinery for cell division is set in motion. The end result of the MAP kinase cascade is activation of a transcription factor. Receptor 1 Ras GDP 2 4 5 Growth factor Ras GTPSee 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. Cyclin Serine Lysine Aspartic "Acid Lysine -OH NH3t -Coo NH3+ NH3 + -OH Aspartic Aad Aspartic Acid /Lysine Serine сок
