GC (Glycocorticoids) binds to the glucocorticoid receptor (GR), which leads to the transcription of a series of genes (PC, PCK1, FBP1, PFKFB1, G6PC and G6P transporter (SLC37A4)) involved in gluconeogenesis. What type of receptor is GR? Where would you expect the activated GR to be located to enhance the expression of the gluconeogenic genes? Which cis-acting elements are used by GR as an activator to turn gene transcription “on”?
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- GC (Glycocorticoids) binds to the glucocorticoid receptor (GR), which leads to the transcription of a series of genes (PC, PCK1, FBP1, PFKFB1, G6PC and G6P transporter (SLC37A4)) involved in gluconeogenesis.
- What type of receptor is GR?
- Where would you expect the activated GR to be located to enhance the expression of the gluconeogenic genes?
- Which cis-acting elements are used by GR as an activator to turn gene transcription “on”?
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- Briefly describe the following properties of the Rab and Arf GTPases: a) Size, structure and cellular localization (for structure I want to know if they are lipidated and any other unique features) , b) How are they activated and inactivated (i.e. include the GEFs and GAPs), c). Give an example of downstream cellular effects.Signal-transducing heterotrimeric G proteins consist of three subunits designated α, β, and γ. The Gα subunit is a GTPase switch protein that cycles between active and inactive states depending on whether it is bound to GTP or to GDP. Review the steps for ligand-induced activation of effector proteins mediated by the heterotrimeric G proteins. Suppose that you have isolated a mutant Gα subunit that has an increased GTPase activity. What effect would this mutation have on the G protein and the effector protein?In response to a hormone secreted by a cell of the opposite mating type, a yeast cell undergoes a complex series of physiological changes involving the activity of about 200 genes and cytoplasmic proteins. They include blockingDNA synthesis, growing toward the mating partner, fusion of the plasma membranes of the two cells, and fusion of their nuclear membranes. Explain how all these events can be controlled through a complex signaling cascade that is triggered by the binding of the hormone to a G protein–linkedreceptor.
- Explain why in cells that are genetically NF1–/–, basal levels of GTP-bound activated Ras are higher than normal and respond to growth factor stimulation by increasing rapidly to far higher levels.A certain group of Brec-MUT cells expresses low levels of protein A, unlike the high expression levels of most Brec-MUT cells. Researchers determine that the cells have an excess of ATP and that there are no mutations in the gene encoding protein A. Describe a change in the Brec signaling pathway that would lead to the decreased expression of protein A even in the presence of Brec-MUT. Explain why B is able to bind to Brec but not to A.Phorbol esters have been observed to induce the transcription of AP-1–influenced genes. Explain how this processcould occur. What are the consequences of AP-1 transcription? What role does intermittent exposure to phorbol estershave on an individual’s health?
- RTKs are receptors made of an extracellular ligand binding domain and an intracellular kinase domain (see image). Insulin binds to its RTK Insulin receptor, causing an increase in glucose absorption and storage in liver cells. EGF binds to its own RTK, EGFR and promotes cell growth through the Ras pathway. a) Explain why the same type of tyrosine kinase in two RTKs can lead to very different cellular responses. Give an example of potential cellular outputs for each of these two RTKs.What effect does binding of the IRF protein to the IRE in the mRNA encoding ferritin have on the production of ferritin? Briefly explain why this effect is observed.Aberrant signaling through the Ras-BRaf-MAPK signal transduction pathway drives many cancers. This makes the pathway an attractive drug target, and many small molecules have been developed that target either Ras, BRaf or MAPK. In malignant melanoma, one mutation in particular, where valine 600 of Braf is mutated to a glutamic acid (V600E), is found in the majority of cases. This mutation makes BRaf activation independent of upstream Ras activity. Would a small molecule that targets Ras be effective in a melanoma case driven by Braf V600E? Explain your answer.
- The ras protein is a mutated G protein that lacks GTPase activity. How does the absence of this activity affect the adenylyl cyclase pathway?Does adenylate cyclase become more active when the inhibitory (Gia) protein is mutated and increases its intrinsic GTPase activity?Now read this abstract from a 2013 journal article What is the authors' explanation of how Gal80p works? Note UASG from the question above is the same as UASGAL The DNA-binding transcriptional activator Gal4 and its regulators Gal80 and Gal3 constitute a galactose-responsive switch for the GAL genes of Saccharomyces cerevisiae. Gal4 binds to GAL gene UASGAL. (upstream activation sequence in GAL gene pro- moter) sites as a dimer via its N-terminal domain and activates transcription via a C-terminal transcription activation domain (AD). In the absence of galactose, a Gal80 dimer binds to a dimer of Gal4, masking the Gal4AD. Galactose triggers Gal3-Gal80 interaction to rapidly initiate Gal4-mediated transcription activation. Just how Gal3 alters Gal80 to relieve Gals0 inhibition of Gal4 has been unknown, but previous analyses of Gal80 mutants suggested a possible competition between Gal3-Gal80 and Gal80 self-association interactions. Here we assayed Gal80-Gal80 interactions and tested for…