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)

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)

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter9: Cell Communication

Section: Chapter Questions

Problem 1VCQ: Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is...

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Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is permanently activated, resulting in unregulated cell division. Lapatinib, a drug used to treat breast cancer, inhibits HER2 receptor tyrosine kinase autophosphorylation (the process by which the receptor adds phosphates onto itself), thus reducing tumor growth by 50 percent. Besides autophosphorylation, which of the following steps would be inhibited by Lapatinib? Signaling molecule binding, dimerization, and the downstream cellular response. Dimerization, and the downstream cellular response. The downstream cellular response. Phosphatase activity, dimerization, and the downsteam cellular response.
Why is the GTPase activity of G proteins crucial to the proper functioning of a cell? Why have G proteins not evolved to catalyze GTP hydrolysis more efficiently?
What is meant by intrinsic GTPase activity? Exchange of GDP for GTP on the a-subunit of the G protein Inhibition of GBCR receptor activity Activation of Adenylyl Cyclades Breakdown of cAMP by phosphodiesterase Spontaneous hydrolysis of GTP on the a-subunit of the G-protein
If you have a protein kinase that is regulated by both small molecule inhibitors as well as by phosphorylation, and is part of a cooperative enzyme complex that works as part of a larger pathway involving kinase and GTPase proteins please explain where on this protein regulation could occur, how different types of inhibition could control the function of the protein as well as the function of the complex, and how the protein could regulate other proteins. (This question was previously answered but it was answered incompletely mentioning an herbicide developed in the 1950's. Apparently, it was a plagiarized excerpt from an NCBI article. This is a repost for a full and complete answer. Thank you so much for your help! :) )
Protein phosphorylation is commonly involved with all of thefollowing except(A) activation of receptor tyrosine kinases.(B) activation of protein kinase molecules.(C) activation of G protein-coupled receptors.(D) regulation of transcription by signaling molecules.
In which condition a trimeric G protein is activated by a cell-surface receptor,a. the a subunit exchanges its bound GDP for GTP.b. the B subunit exchanges its bound GDP for GTP.c. the GDP bound to the a subunit is phosphorylated to form bound GTP.d. it dissociates into a free B subunit and an ay subunit.e. it dissociates into an active a subunit and in inactive By subunit.
To move in a specific direction, a migrating cell must use extracellular cues to establish which portion of the cell will act as the front and which will act as the back. Describe how small GTPase proteins appear to be involved in the signaling pathways used by migrating cells to determine direction of movement.
Cholera toxins, produced by the pathogenic bacteria Vibrio cholerae, disrupt G Protein Coupled Receptor (GPCR) signaling pathways. They interfere with... the ability of the beta subunit of a G protein to bind to the GPCR the ability of the gamma subunit of a G protein to exchange GDP for GTP the ability of the beta subunit of a G protein to bind to an effector protein the ability of the alpha subunit of a G protein to hydrolyze GTP to GDP
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.
After the GEF causes the GTPase to release its GDP, why is the nucleotide-binding site immediately filled by a GTP molecule rather than a GDP molecule?
What are the three main parts of a signaling pathway? Give a detailed specific example, such as how epinephrine signals for rapid digestion of glycogen in liver cells.
Why is it important that the approximately 60 different Rab GTPases in humans are associated with different intracellular membranes?