BIOLOGY 2E
2nd Edition
ISBN: 9781506699851
Author: OpenStax
Publisher: XANEDU PUBLISHING
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Chapter 9, Problem 2VCQ
Figure 9.10 In certain cancers, the GTPase activity of the RAS G-protein is inhibited. This means that the RAS protein can no longer hydrolyze GTP into GDP What effect would this have on downstream cellular events?
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The ras protein is a mutated G protein that lacks GTPase activity. How does the absence of this activity affect the adenylyl cyclase pathway?
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)
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 GEF
Chapter 9 Solutions
BIOLOGY 2E
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- 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…arrow_forwardRTKs 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.arrow_forwardWhich of the following mutations would produce a form of the Ras protein that would be more difficult to inactivate than normal Ras? Briefly explain your reasoning.(i) A mutation that allows Ras to cleave (hydrolyze) GTP more rapidly than usual(ii) A mutation that causes Ras to bind Ras-GAP more tightly than usual(iii) A mutation that causes Ras to cleave (hydrolyze) GTP more slowly than usualarrow_forward
- Even in the presence of a Ras-GAP, a single amino acid change in as renders it incapable of hydrolyzing GTP. This mutation is known as Ras+ and is a cancer-causing mutation. What effect do you think this mutation will have on signaling downstream of Ras+? Why? a)A mutation would turn on the signaling pathway all of the time. b)Even if a route is mutated, it can still be turned on or off. c)Due to a mutation, the signaling pathway would always be off.arrow_forwardBriefly describe the following properties of the Ras 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 effector proteins, d). Are they or could they be involved in human cancer.arrow_forwardRGS proteins accelerate the GAP activity of Gα subunits. What is the direct result of this GAP activity? - hydrolysis of GTP, resulting in a GDP-bound Gα - phosphorylation of GDP to GTP, resulting in a GTP-bound Gα - an exchange of GTP for GDP bound to Gα - an exchange of GDP for GTP bound to Gαarrow_forward
- 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.arrow_forwardMutation in the fibroblast growth factor receptor (FGFR) gene results in achondroplasia (dwarfism), which is a dominant condition caused by a single base substitution (GGG>AGG) that changes the amino acid glycine at position 480 to arginine (G480R) in the FGFR protein. FGFR is normally active when FGF binds to it, but the mutant FGFR is always on to stimulate signaling that inhibits excessive bone growth. How can gene therapy be used to treat achondroplasia? Select all that apply. RNAi that knocks down the mutant FGFR expression Adeno-associated viral (AAV) vector that carries the wild-type FGFR Retroviral vector that carries the wild-type FGFR CRISPR with the wild-type FGFR donor DNAarrow_forwardMany 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 correctarrow_forward
- The G protein coupled receptor (GPCR) pathway elicits diverse intracellular responses in different cells. The basic steps of GPCR signaling are outlined in this diagram. Which of the following statements correctly describes the process of GPCR signaling? The GPCR activation is reversible after the signal of the ligand diminishes. The membrane-embedded enzyme uses GTP as a secondary messenger to initiate gene expression. The ligand attaches to both the GPCR and the membrane-embedded enzyme to activate the GPCR pathway. The ligand-bound GPCR sends a GTP molecule to an enzyme in the membrane and switches it into an active state.arrow_forwardGTP 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.arrow_forwardIf a cell expresses a dominant-negative tyrosine-kinase-linked receptor (RTK) that lacks the kinase domain, which of the following will still happen in response to a growth factor that binds the RTK? A Receptor cross-phosphorylation. Activation of target proteins by Ras. C) Receptor dimerization. D) Binding of the growth factor to its receptor. Interaction of Ras with the activated receptor. Barrow_forward
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