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What would most likely occur if glucosyltransferase were removed from the ER? BiP binding to misfolded proteins would increase and the ER would fill up with misfolded proteins Incompletely folded proteins would traffic to the Golgi ATF6 would leave the ER, activate in the Golgi, and initiate transcription of stress-relieving genes PERK would become active and inactivate elF2alpha

What would most likely occur if glucosyltransferase were removed from the ER? BiP binding to misfolded proteins would increase and the ER would fill up with misfolded proteins Incompletely folded proteins would traffic to the Golgi ATF6 would leave the ER, activate in the Golgi, and initiate transcription of stress-relieving genes PERK would become active and inactivate elF2alpha

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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**Question:** What would most likely occur if glucosyltransferase were removed from the ER? **Options:** 1. **BiP binding to misfolded proteins would increase and the ER would fill up with misfolded proteins** - This option suggests that the absence of glucosyltransferase would lead to an accumulation of misfolded proteins in the endoplasmic reticulum (ER), binding more BiP chaperone proteins. 2. **Incompletely folded proteins would traffic to the Golgi** - This implies that, without glucosyltransferase, partially folded proteins might begin moving from the ER to the Golgi apparatus. 3. **ATF6 would leave the ER, activate in the Golgi, and initiate transcription of stress-relieving genes** - This option describes a stress response where ATF6 moves from the ER to the Golgi, activating genes that help mitigate stress. 4. **PERK would become active and inactivate eIF2alpha** - Here, the removal of glucosyltransferase could trigger the activation of PERK, which then inhibits eIF2alpha as part of a stress response mechanism. ***Note:*** The question explores the cellular response mechanisms related to protein folding and stress in the endoplasmic reticulum. Each option reflects a different aspect of how cells handle misfolded proteins and associated stress.
Transcribed Image Text:**Question:** What would most likely occur if glucosyltransferase were removed from the ER? **Options:** 1. **BiP binding to misfolded proteins would increase and the ER would fill up with misfolded proteins** - This option suggests that the absence of glucosyltransferase would lead to an accumulation of misfolded proteins in the endoplasmic reticulum (ER), binding more BiP chaperone proteins. 2. **Incompletely folded proteins would traffic to the Golgi** - This implies that, without glucosyltransferase, partially folded proteins might begin moving from the ER to the Golgi apparatus. 3. **ATF6 would leave the ER, activate in the Golgi, and initiate transcription of stress-relieving genes** - This option describes a stress response where ATF6 moves from the ER to the Golgi, activating genes that help mitigate stress. 4. **PERK would become active and inactivate eIF2alpha** - Here, the removal of glucosyltransferase could trigger the activation of PERK, which then inhibits eIF2alpha as part of a stress response mechanism. ***Note:*** The question explores the cellular response mechanisms related to protein folding and stress in the endoplasmic reticulum. Each option reflects a different aspect of how cells handle misfolded proteins and associated stress.
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