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Which of the following statements regarding signaling in normal cells and cancer cells is false? a. In normal cells, RTK transphosphorylation is strictly dependent on ligand binding. Ligand binding promotes a conformational change in the RTKS that is required for dimerization, and dimerization is required for transphosphorylation. b. Cancers cells that over-express RTK's can respond to tiny amounts of ligand, and in some instances signaling can be ligand-independent. c. Cancer cells that have established several autocrine signaling loops have a poor prognosis, because these cells have enabled multiple independent mitogenic signal transduction pathways. 4 d. The extracellular ectodomains of all RTKs are highly conserved in primary sequence and structure. e RTKs have a hydrophilic extracellular ectodomain, and hydrophobic transmembrane domain, and a hydrophilic cytoplasmic domain, which contains the catalytic portion of the protein.

Which of the following statements regarding signaling in normal cells and cancer cells is false? a. In normal cells, RTK transphosphorylation is strictly dependent on ligand binding. Ligand binding promotes a conformational change in the RTKS that is required for dimerization, and dimerization is required for transphosphorylation. b. Cancers cells that over-express RTK's can respond to tiny amounts of ligand, and in some instances signaling can be ligand-independent. c. Cancer cells that have established several autocrine signaling loops have a poor prognosis, because these cells have enabled multiple independent mitogenic signal transduction pathways. 4 d. The extracellular ectodomains of all RTKs are highly conserved in primary sequence and structure. e RTKs have a hydrophilic extracellular ectodomain, and hydrophobic transmembrane domain, and a hydrophilic cytoplasmic domain, which contains the catalytic portion of the protein.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Which of the following statements regarding signaling in normal cells and cancer cells is false? a. In normal cells, RTK transphosphorylation is strictly dependent on ligand binding. Ligand binding promotes a conformational change in the RTKS that is required for dimerization, and dimerization is required for transphosphorylation. b. Cancers cells that over-express RTK's can respond to tiny amounts of ligand, and in some instances signaling can be ligand-independent. c. Cancer cells that have established several autocrine signaling loops have a poor prognosis, because these cells have enabled multiple independent mitogenic signal transduction pathways. 4 d. The extracellular ectodomains of all RTKS are highly conserved in primary sequence and structure. e. RTKS have a hydrophilic extracellular ectodomain, and hydrophobic transmembrane domain, and a hydrophilic cytoplasmic domain, which contains the catalytic portion of the protein.
Transcribed Image Text:Which of the following statements regarding signaling in normal cells and cancer cells is false? a. In normal cells, RTK transphosphorylation is strictly dependent on ligand binding. Ligand binding promotes a conformational change in the RTKS that is required for dimerization, and dimerization is required for transphosphorylation. b. Cancers cells that over-express RTK's can respond to tiny amounts of ligand, and in some instances signaling can be ligand-independent. c. Cancer cells that have established several autocrine signaling loops have a poor prognosis, because these cells have enabled multiple independent mitogenic signal transduction pathways. 4 d. The extracellular ectodomains of all RTKS are highly conserved in primary sequence and structure. e. RTKS have a hydrophilic extracellular ectodomain, and hydrophobic transmembrane domain, and a hydrophilic cytoplasmic domain, which contains the catalytic portion of the protein.
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