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- GTP is an important high-energy molecule that facilitates the activation of many cellular sig- nal transduction pathways. Certain genetic dysfunctions can inhibit the ability of a cell to synthesize GTP. Which of the following describes the most direct result of GTP synthesis inhibition? A B с D The cell would be able to carry out reception and transduction but would not be able to produce the cellular response in the relevant signal transduction pathway. The G protein-coupled receptor will not be able to bind corresponding ligands, inhibiting the reception components of the relevant signal transduction pathway. The cell will use ATP instead of GTP to activate the G protein on the intracellular region of the G protein-coupled receptor. The cell would not be able to activate G proteins on the intracellular regions of G pro- tein-coupled receptors.The above answer did not address the question in the sense that the answer did not indicate which protein involved in the pathways could be measured in the nucleus of cells and be confident in the results? I reiterate the question as follows: You want to do a single Western blot to measure changes in signaling activity, regardless of which pathway is being activated. For which protein involved in these pathways could you measure the levels in the nucleus of cells and be confident in your results? Why?Compare and contrast GPCR and RTK signaling. What role does GTP play in each? What role does phosphorylation play? How do these two signaling types compare to steroid signaling with respect to gene activation?
- 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.The diagram below shows a closeup of regulatory proteins binding to one of the UASG elements near the GAL7, GALI0, and GALI genes, which code for the protein products needed for yeast to use the sugar galactose. The red triangle symbolizes an "effector" molecule that binds to Gal80p. In this hypothesis (which has since been shown to be incorrect), what could be happening to Gal80p when it is bound to the effector molecule that causes it to change its position and uncover the Gal4p transcriptional activation domain. Hint: think about what effector molecules do upon binding to proteins such as the the Lac repressor protein or the CAP protein. Galactose absent, glucose absent Gal80p. _Activation domain Gal4p dimer -Binding domain UASG Galactose present, glucose absent Activation domain Gal80p- Binding domain UASG For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac).To understand how a signaling pathway works, it is often useful to isolate the cell-surface receptor and to measure the activity of downstream effector proteins under different conditions. How could you use affinity chromatography to isolate a cell-surface receptor?
- Why is the GTPase activity of G proteins crucial to the proper functioning of a cell? Propose a theory as to why G proteins have not evolved to catalyze GTP hydrolysis more efficiently.In the case of GPCR (G protein coupled receptor) signaling pathways, which of the following statements is INCORRECT? The gamma subunit of the trimeric G protein has a transmembrane domain whereas the alpha and beta subunits are peripheral proteins If G alpha was locked in a GTP bound state, it would be bound to the effector enzyme rather than to the beta and gamma subunits. In some but not all signaling pathways, when the beta and gamma subunits are separated from alpha - the beta/gamma pair can also stimulate the activation of effectorsThe oscillatory clock that drives somite forma-tion in vertebrates involves three essential componentsHer7 (an unstable repressor of its own synthesis), Delta (atransmembrane signaling molecule), and Notch (a trans-membrane receptor for Delta). Notch is bound by Delta onneighboring cells, activating the Notch signaling pathway,which then activates Her7 transcription. Normally, thissystem works flawlessly to create sharply defined somites(Figure Q21–2A). In the absence of Delta, however, onlythe first five somites form normally, and the rest are poorlydefined (Figure Q21–2B). If a pulse of Delta is suppliedlater, somite formation returns to normal in the regionswhere Delta was present (Figure Q21–2C). A diagram ofthe connections between the components of the clockand how they interact in adjacent cells is shown in FigureQ21–2D. In the absence of Delta, why do the cells becomeunsynchronized? What is it about the presence of Deltathat keeps adjacent cells oscillating in synchrony?
- 3) The “Met" receptor is a membrane receptor protein responsible for initiating signal transduction pathways that cause cells to divide, among other things. After the Met receptor has been stimulated by its specific growth factor, another protein called c- Cbl will bind to the Met receptor. C-Cbl will then attach a chain of small proteins called ubiquitin to the Met receptor. These chains of ubiquitin help the cell recognize that the Met receptor should undergo receptor-mediated endocytosis, which eventually leads to the destruction of the Met receptor. Circle any answer or answers that include mutations that could cause the cell to potentially become a cancer cell. A) a mutation causing there to be too much ubiquitin protein produced. B) a mutation causing c-Cbl to be inactivated. C) a mutation causing ubiquitin to be inactivated. D) a mutation causing there to be too few Met receptors produced. E) a mutation causing the Met receptor to no longer be able to bind to its growth factor.…Researchers have found that a certain signal transduction pathway, illustrated in the figure below, may be responsible for the development of cancer in pancreatic cells. In normal pancreatic cells, where the pathway remains inactive, a membrane-bound receptor called Ptc inhibits a downstream protein known as Smo. The inhibition of Smo blocks the activa- tion of a complex of proteins known as the HSC, which results in the cleaving of one of its proteins called Ci. The cleaving of Ci, in turn, prevents the pathway from initiating the syn- thesis of division-facilitating enzymes. A Ptc B Smo с inhibition D A model of a Ptc signal transduction pathway under normal conditions. HSC Ci cleavage A certain protein called the Hedgehog protein (Hh) is found to activate this signal transduction pathway and trigger uninterruptable cell division. cell division not initiated Which of the following describes the most plausible mechanism by which Hh triggers uninterruptable cell division? Hh binds to…There is now significant evidence to support the existence of cytoneme-mediated delivery of signaling ligands. What is their mechanism of action, and what is the relevance of this discovery to embryonic development?