The G-protein Ras is involved in proliferative signaling, and is mutated is a large fraction of human cancers. Almost all mutations in Ras mutate the glycine at codon 12. These mutations lock Ras in an active conformation. How will the GTPase activity of a Ras protein with a G12 mutation compare to a normal Ras protein without the mutation? (10 words maximum)
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The G-protein Ras is involved in proliferative signaling, and is mutated is a large fraction of human cancers. Almost all mutations in Ras mutate the glycine at codon 12. These mutations lock Ras in an active conformation. How will the GTPase activity of a Ras protein with a G12 mutation compare to a normal Ras protein without the mutation? (10 words maximum)
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- GTP binding proteins are molecular switches. How do GTP binding proteins work? Provide two examples of GTP binding proteins that function in intracellular protein transport. Make a drawing that illustrates the function of each of these proteins in their respective roles. Predict the direct outcome of a mutation that: Inhibits GTPase activity Inhibits interaction with the GEFSome strains of bacteria or microorganisms have developed toxins that can modify the activity of the alpha subunit of G proteins which results in disease. For ex. cholera toxin, produced by Vibrio cholerae, causes ADP ribosylation of the stimulatory Gαs subunit of G proteins. This modification abolishes the GTPase of Gαs, and results in an αs subunit that is always in the “on” or active state. It results in continuous stimulation of adenylyl cyclase (AC). The main cells affected by this are the epithelial cell in gastrointestinal tract. Knowing this altered activity of AC, explain why patients affected by this toxin experience severe diarrhea and dehydration that may result in death.Caspase proteins are enzymes known to play a role in programmed cell death (apoptosis) and the inflammatory response. Apoptotic caspases are subcategorized into initiator and executioner caspases. Initiator caspases produce a chain reaction that activates executioner caspases. Caspase 9 is a kind of initiator caspase and caspase 3 is a kind of executioner caspase that plays a direct role in degrading cellular components.Apoptosis can be activated by internal (intrinsic) cellular mechanisms or external (extrinsic) signals. The extrinsic apoptotic pathway begins with the reception of a signal at the death receptors and the intrinsic apoptotic pathway begins with the permeabilization of the mitochondria. Both apoptotic caspase pathways are shown in Figure 1. Caspase proteins have been implicated in the premature death of cornea endothelial tissue being stored for transplant. To investigate the effect of caspases 3 and 9 on tissue degradation, scientists monitored the endothelial cell…
- Caspase proteins are enzymes known to play a role in programmed cell death (apoptosis) and the inflammatory response. Apoptotic caspases are subcategorized into initiator and executioner caspases. Initiator caspases produce a chain reaction that activates executioner caspases. Caspase 9 is a kind of initiator caspase and caspase 3 is a kind of executioner caspase that plays a direct role in degrading cellular components.Apoptosis can be activated by internal (intrinsic) cellular mechanisms or external (extrinsic) signals. The extrinsic apoptotic pathway begins with the reception of a signal at the death receptors and the intrinsic apoptotic pathway begins with the permeabilization of the mitochondria. Both apoptotic caspase pathways are shown in Figure 1 Caspase proteins have been implicated in the premature death of cornea endothelial tissue being stored for transplant. To investigate the effect of caspases 3 and 9 on tissue degradation, scientists monitored the endothelial cell…Caspase proteins are enzymes known to play a role in programmed cell death (apoptosis) and the inflammatory response. Apoptotic caspases are subcategorized into initiator and executioner caspases. Initiator caspases produce a chain reaction that activates executioner caspases. Caspase 9 is a kind of initiator caspase and caspase 3 is a kind of executioner caspase that plays a direct role in degrading cellular components.Apoptosis can be activated by internal (intrinsic) cellular mechanisms or external (extrinsic) signals. The extrinsic apoptotic pathway begins with the reception of a signal at the death receptors and the intrinsic apoptotic pathway begins with the permeabilization of the mitochondria. Both apoptotic caspase pathways are shown in Figure 1. Caspase proteins have been implicated in the premature death of cornea endothelial tissue being stored for transplant. To investigate the effect of caspases 3 and 9 on tissue degradation, scientists monitored the endothelial cell…Caspase proteins are enzymes known to play a role in programmed cell death (apoptosis) and the inflammatory response. Apoptotic caspases are subcategorized into initiator and executioner caspases. Initiator caspases produce a chain reaction that activates executioner caspases. Caspase 9 is a kind of initiator caspase and caspase 3 is a kind of executioner caspase that plays a direct role in degrading cellular components.Apoptosis can be activated by internal (intrinsic) cellular mechanisms or external (extrinsic) signals. The extrinsic apoptotic pathway begins with the reception of a signal at the death receptors and the intrinsic apoptotic pathway begins with the permeabilization of the mitochondria. Both apoptotic caspase pathways are shown in Figure 1. Caspase proteins have been implicated in the premature death of cornea endothelial tissue being stored for transplant. To investigate the effect of caspases 3 and 9 on tissue degradation, scientists monitored the endothelial cell…
- Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, has the highest specificity in binding to the target Protein J?Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, may be expected to be the most potent or have the highest activity against cancer? Explain. b. Which of the ligands, based on the table, may be expected to be least toxic to normal cells? Explain.Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: Describe the relative binding affinities of Ligand A to Protein K and to the active and inactive forms of Protein J. Determine which will Ligand A bind with the highest, medium, and lowest affinity.
- G protein coupled receptors play an important role in signal transduction in many cells. Label the four essential components of the G protein coupled receptor signaling system (blanks a-d in the picture) by choosing from the menus below. a b b Each answer will be used at most once, while some will not be used at all (select one for each): Group of answer choices transcription factor с transcription factor Show Transcribed Text d transcription factor B C. transcription factor G protein second messenger G protein second messenger IE G protein second messenger G protein second messenger receptor receptor receptor receptor enzyme enzyme enzyme enzyme steroid hormone steroid hormone steroid hormone steroid hormoneMany cellular processes require the hydrolysis of GTP to GDP. However, unlike ATP, GTP hydrolysis is often not used as an energy source for the cell, but rather, is associated with a group of enzymes called GTPases. Which of the following statements about GTP and GTPases is correct? 1. GTPase activating protein (GAP) binds to GTPase when it is in the active state. 2. The exchange factor GEF binds GTP directly and delivers it to the GTPase. 3. The "switching" behaviour of GTPase is because GTP hydrolysis causes the enzyme to change shape. 4. Structural differences in the terminal phosphate group explains why ATP hydrolysis releases energy and GTP does not. O 1,2 and 3 O 1 and 3 O 2 and 4 O 4 only O All of 1,2.3 and 4 are correctRTKs 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.