NIH VideoCast - Ubiquitination and deubiquitination: a Yin-Yang cycle in protein quality control at the endoplasmic reticulum

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Ubiquitination and deubiquitination: a Yin-Yang cycle in protein quality control at the endoplasmic reticulum

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Air date:	Friday, April 12, 2013, 12:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 569 (49 Live, 520 On-demand)
Category:	NIH Director's Seminars
Runtime:	01:10:04
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Director's Seminar Series The endoplasmic reticulum (ER) is the major site of protein biosynthesis in eukaryotes. Polypeptides entering the ER frequently encounter folding problems, resulting in aggregation-prone, misfolded proteins. To preserve ER homeostasis, eukaryotic cells have evolved a conserved quality control pathway termed ER-associated protein degradation (ERAD) or retrotranslocation, which eliminates unwanted proteins of the ER by exporting them into the cytosol for degradation by the ubiquitin proteasome system. Defects in ERAD result in accumulation of misfolded proteins and cause ER stress. ER stress has been implicated in the pathogenesis of many human diseases including type 2 diabetes and several types of neurodegenerative diseases. The retrotranslocation system is also hijacked by certain viruses to destroy folded cellular proteins essential for anti-viral defense. This allows viruses to evade host immune surveillance. The molecular mechanism by which retrotranslocated substrates are targeted to the proteasome has been elusive. Recent studies from my laboratory reveal a complex interplay between ubiquitin ligases, deubiquitinating enzymes, and a chaperone holdase in this process.

NLM Title:	Ubiquitination and deubiquitination : a Yin-Yang cycle in protein quality control at the endoplasmic reticulum / Yihong Ye.
Author:	Ye, Yihong. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): Director's Seminar Series The endoplasmic reticulum (ER) is the major site of protein biosynthesis in eukaryotes. Polypeptides entering the ER frequently encounter folding problems, resulting in aggregation-prone, misfolded proteins. To preserve ER homeostasis, eukaryotic cells have evolved a conserved quality control pathway termed ER-associated protein degradation (ERAD) or retrotranslocation, which eliminates unwanted proteins of the ER by exporting them into the cytosol for degradation by the ubiquitin proteasome system. Defects in ERAD result in accumulation of misfolded proteins and cause ER stress. ER stress has been implicated in the pathogenesis of many human diseases including type 2 diabetes and several types of neurodegenerative diseases. The retrotranslocation system is also hijacked by certain viruses to destroy folded cellular proteins essential for anti-viral defense. This allows viruses to evade host immune surveillance. The molecular mechanism by which retrotranslocated substrates are targeted to the proteasome has been elusive. Recent studies from my laboratory reveal a complex interplay between ubiquitin ligases, deubiquitinating enzymes, and a chaperone holdase in this process.
Subjects:	Endoplasmic Reticulum--physiology Ubiquitin--metabolism Ubiquitination--physiology
Publication Types:	Lecture Webcast

NLM Classification:	QU 55
NLM ID:	101607229
CIT Live ID:	12551
Permanent link:	https://videocast.nih.gov/watch=12551

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