Indicate whether each of the following mutations would likely promote (P) or inhibit (I) apoptosis in cells harboring the mutation(s). Your answer would be a four-letter string composed of letters P and I only, e.g. PPPI. (  ) Mutations in the pro-apoptotic effector Bcl2 family proteins Bax and Bak that prevent their association with the outer mitochondrial membrane. (  ) A mutation in the BIR domain of the IAP protein DIAP1 that prevents binding to either caspases or anti-IAP proteins. (  ) A mutation in the anti-IAP protein Reaper that prevents its binding to the IAP proteins. (  ) A mutation in the CARD domain of caspase-9 that prevents its binding to Apaf1.

The actin-nucleating protein formin has flexible “whiskers” containing binding sites that help recruit actin subunits in order to enhance polymerization by this protein. What protein would you expect to bind to these sites?

The following schematic diagram shows the activation of M-Cdk in mitosis. Indicate which proteins below correspond to those indicated as A to D in the diagram. Your answer would be a four-letter string. (  ) Wee1 (  ) CAK (  ) Cdc25 (  ) M-cyclin

Consider the in vitro motility assay using purified kinesin and purified polymerized microtubules shown in the Figure below. The three panels are images taken at 1-second intervals. In this figure, three microtubules have been numbered to make it easy to identify them. Which of the following statements about this assay is FALSE?

G-protein-coupled receptors (GPCRs) all have a similar structure with ____________ transmembrane domains. When a GPCR binds an extracellular signal, an intracellular G protein, composed of _________ subunits, becomes activated. _________ of the G-protein subunits are tethered to the plasma membrane by short lipid tails. When unstimulated, the α subunit is bound to ________, which is exchanged for _______ on stimulation. The intrinsic ________ activity of the α subunit is important for inactivating the G protein. _______ inhibits this activity of the α subunit, thereby keeping the subunit in an active state.   adenylyl cyclase                 cholera toxin           GTPase  AMP                                        diacylglycerol           phosphodiesterase ATP                                          five                                   seven  ATPase                                  four                                  three Ca2+                                                    GDP                                  twelve cAMP                                   GTP                                   two

What is the effect of defective or missing N-acetylglucosamine phosphotransferase on lysosomal protein sorting?

Which of the following choices reflects the appropriate order of locations through which a protein destined for the plasma membrane travels?

You have created a green fluorescent protein (GFP) fusion to a protein that is normally secreted from yeast cells. Because you have learned about the use of temperature-sensitive mutations in yeast to study protein and vesicle transport, you obtain three mutant yeast strains, each defective in some aspect of the protein secretory process. Being a good scientist, you of course also obtain a wild-type control strain. You decide to examine the fate of your GFP fusion protein in these various yeast strains and engineer the mutant strains to express your GFP fusion protein. However, in your excitement to do the experiment, you realize that you did not label any of the mutant yeast strains and no longer know which strain is defective in what process. You end up numbering your strains with the letters A through D, and then you carry out the experiment anyway, obtaining the results shown in Figure below (the black dots represent your GFP fusion protein). Name the protein that is defective in each of these strains. Remember that one of these strains is your wild-type control.

Indicate true (T) and false (F) statements below regarding signaling. Your answer would be a four-letter string composed of letters T and F only, e.g. TTTF. (  ) Since multicellularity evolved before the divergence of the plant and animal lineages, plants have homologs of most animal signaling proteins, such as nuclear receptors, Ras, JAK, and Notch. (  ) Receptor tyrosine kinases are the largest class of cell-surface receptors in plant cells. (  ) Animals use cyclic GMP, NO, and Ca2+ for cell signaling. (  ) Receptor tyrosine kinases are the most abundant type of receptors signaling proliferation in animal cells.

The rod photoreceptors in the eye are extremely sensitive to light. The cells sense light through a signal transduction cascade involving light activation of a GPCR that activates a G protein that activates cyclic GMP phosphodiesterase. How would you expect the addition of the following drugs to affect the light-sensing ability of the rod cells? Explain your answers. a drug that inhibits cyclic GMP phosphodiesterase a drug that is a nonhydrolyzable analog of GTP