ERAD, or ER associated degradation, is a quality control measure with the following function: O A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly O B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol OC. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER O D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles for degradation

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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ERAD, or ER associated degradation, is a quality control measure with the following function:
A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly
B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol
C. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER
D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles
for degradation
Transcribed Image Text:ERAD, or ER associated degradation, is a quality control measure with the following function: A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol C. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles for degradation
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