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- 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.Describe e-cadherins' ligand affinity properties. What is e-cadherins' role in cell sorting? Have detail.Consider a mutant version of a cell-surface receptor. This mutation does not affect the amount of receptor produced by the cell, but it does decrease the efficiency with which the receptor is incorporated to form endocytic vesicles. Based on the mechanism of vesicle formation & cargo loading, what interaction is most likely to be disrupted by this mutation in the cytoplasmic domain of the receptor? In other words, what might now be unable to effectively bind to the receptor? Briefly explain your reasoning.
- Animal cells utilize rapid increases in cytosolic Ca++ ion concentration to respond to certain extracellular signals. This requires keeping the cytosolic Ca++ ion concentration very low in the absence of signal (when the cell is “at rest”) and increasing the cytosolic Ca++ ion concentration when a signal is detected. Propose a mechanism by which the action of Ca++ transport proteins in the plasma membrane can account for the reversibility of Ca++ levels in the cytosol. Be sure to indicate whether active or passive transport is involved as well as the type of transport protein (channel or carrier) responsible.In eukaryotic cells secreted proteins are targeted first to the endoplasmic reticulum and then pass through the Golgi, before being released from secretory vesicles into the extracellular space. A much simpler route would be for ribosomes synthesising secretory proteins to be targeted to a translocon in the plasma membrane, with the protein being secreted directly as it is translated. List three potential advantages of the former, more circuitous, route for protein secretion over the simpler, more direct, alternative route suggested.You perform a competition study on a GPCR. You have isolated the plasma membrane from cells which contains the GPCR of interest. If an agonist and an inverse agonist are at equal concentrations in your study but the inverse agonist has a 10 x higher affinity for the receptor than the agonist, what would you expect to be the overall outcome to be? More of the agonist is bound and so most of the receptor is in its active conformation and is stimulated More of the inverse agonist is bound and so most of the receptor is in its inactive conformation and is unstimulated.
- 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.You 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…
- In the lab you will prepare a dye solution to test transmembrane transport into yeast cells. The dye stock solution has a concentration of 5 mM. For your experiment, you want the dye concentration to be at 0.25 mM. You do the dilution with water. Select among the following, which of the following method(s) will give you the correct final concentration of dye? 1) adding 1 ml of stock solution to 19 ml of water. 2) making a 25-fold dilution. 3) adding 100 ml of water to 5 ml of dye stock solution. 4) diluting 3 ml of concentrated dye with water to a final volume of 60 ml. A. All methods are accurate B. only methods 1, 2 and 3 are accurate C. only methods 1, 3 and 4 are accurate D. only methods 1 and 4 are accurate E. only method 3 is accurate F. None of the methods reflect the proper dilution method.(edited) [3:16 PM]Which statement about the M6P receptor is true/accurate? Answers: It is involved in retrieval of ER resident proteins from the Golgi and transport back to the ER. Due to no difference in pH in the lumen of each, it has the same affinity for M6P in the Golgi as in the endosome. Due to a slight difference in pH in the lumen of each, it has a high affinity for M6P in the Golgi and a low affinity for M6P in the endosome. Due to a slight difference in pH in the lumen of each, it has a low affinity for M6P in the Golgi and a high affinity for M6P in the endosome.Select the most accurate explanation for how vesicular transport occurs when a receptor is moving from the plasma memberane to the late endosome/lysosome. A. Endosomes containing the receptor are transported by myosin II walking towards the minus end of microtubules. Endosomes are targeted to the late endosome/lysosome by Rab and SNARES facilitate membrane fusion. B. Endosomes containing the receptor are transported by myosin V walking towards the minus end of microtubules. Endosomes are targeted to the late endosome/lysosome by Rab and SNARES facilitate membrane fusion. OC. Endosomes containing the receptor are transported by dyenin walking towards the minus end of microtubules. Endosomes are targeted to the late endosome/lysosome by Rab and SNARES facilitate membrane fusion. D. Endosomes containing the receptor are transported by kinesin-13 walking towards the plus end of microtubules. Endosomes are targeted to the late endosome/lysosome by clathrin and SNARES facilitate membrane…