Skip Navigation


CIT can broadcast your seminar, conference or meeting live to a world-wide audience over the Internet as a real-time streaming video. The event can be recorded and made available for viewers to watch at their convenience as an on-demand video or a downloadable podcast. CIT can also broadcast NIH-only or HHS-only content.

Bittersweet Roles of O-GlcNAcylation in Diabetes, Alzheimer's Disease and Cancer

Loading video...

311 Views  
   
Air date: Wednesday, December 7, 2011, 3:00:00 PM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 311, (106 Live, 205 On-demand)
Category: WALS - Wednesday Afternoon Lectures
Runtime: 00:54:24
Description: O-GlcNAcylation, the cycling of a N-acetylglucosamine monosaccharide on Ser(Thr) residues of nuclear and cytoplasmic proteins, serves as a nutrient/stress sensor to regulate signaling, transcription and cellular metabolism. Recent phospho- and glycomic approaches have shown that an increase in global O-GlcNAcylation affects phospho-site occupancy at nearly every actively cycling site. A chemico-enzymatic photochemical enrichment method, combined with ETD-mass spectrometry allows detection of O-GlcNAc site occupancy at a level of sensitivity comparable to that possible for phosphorylation. These analyses show that crosstalk between site-specific phosphorylation and O-GlcNAcylation is extensive. Many kinases are both modified and regulated by O-GlcNAcylation. The major sensor of cellular energy state, AMPK is O-GlcNAcylated. AMPK and O-GlcNAc transferase share many substrates and the two systems directly interact. Major signaling cascades (eg. CDK1, aurora kinase, polo kinase) that regulate cell division are strikingly affected by a small change in O-GlcNAcylation. O-GlcNAc is part of the histone code, but many of the O-GlcNAc residues are at sites interacting with DNA in the nucleosome, not in the histone tails. Multiple core ribosome proteins are modified by O-GlcNAc, which plays a role in ribosome biogenesis and assembly. O-GlcNAc cycling is strikingly elevated in most forms of cancer. Excessive O-GlcNAcylation of regulatory proteins appears to underlie "glucose toxicity" associated with diabetes. In the brain, reduced O-GlcNAcylation of many proteins is associated with neurodegenerative disease. Thus, O-GlcNAcylation modulates many signaling cascades and phosphate-mediated molecular switches to "tune" them to be highly responsive to nutrients and stress.

The NIH Wednesday Afternoon Lecture Series includes weekly scientific talks by some of the top researchers in the biomedical sciences worldwide.

For more information, visit:
The NIH Director's Wednesday Afternoon Lecture Series
Debug: Show Debug
NLM Title: Bittersweet roles of o-GlcNAcylation in diabetes, Alzheimer's disease, and cancer [electronic resource] / Gerald W. Hart.
Author: Hart, Gerald W.
National Institutes of Health (U.S.)
Publisher:
Abstract: (CIT): O-GlcNAcylation, the cycling of a N-acetylglucosamine monosaccharide on Ser(Thr) residues of nuclear and cytoplasmic proteins, serves as a nutrient/stress sensor to regulate signaling, transcription and cellular metabolism. Recent phospho- and glycomic approaches have shown that an increase in global O-GlcNAcylation affects phospho-site occupancy at nearly every actively cycling site. A chemico-enzymatic photochemical enrichment method, combined with ETD-mass spectrometry allows detection of O-GlcNAc site occupancy at a level of sensitivity comparable to that possible for phosphorylation. These analyses show that crosstalk between site-specific phosphorylation and O-GlcNAcylation is extensive. Many kinases are both modified and regulated by O-GlcNAcylation. The major sensor of cellular energy state, AMPK is O-GlcNAcylated. AMPK and O-GlcNAc transferase share many substrates and the two systems directly interact. Major signaling cascades (eg. CDK1, aurora kinase, polo kinase) that regulate cell division are strikingly affected by a small change in O-GlcNAcylation. O-GlcNAc is part of the histone code, but many of the O-GlcNAc residues are at sites interacting with DNA in the nucleosome, not in the histone tails. Multiple core ribosome proteins are modified by O-GlcNAc, which plays a role in ribosome biogenesis and assembly. O-GlcNAc cycling is strikingly elevated in most forms of cancer. Excessive O-GlcNAcylation of regulatory proteins appears to underlie "glucose toxicity" associated with diabetes. In the brain, reduced O-GlcNAcylation of many proteins is associated with neurodegenerative disease. Thus, O-GlcNAcylation modulates many signaling cascades and phosphate-mediated molecular switches to "tune" them to be highly responsive to nutrients and stress.
Subjects: Alzheimer Disease
Diabetes Mellitus
Glycosylation
Neoplasms
Publication Types: Lectures
Webcasts
Download: To download this event, select one of the available bitrates:
[256k]  [512k]    How to download a Videocast
Caption Text: Download Caption File
NLM Classification: WK 810
NLM ID: 101576000
CIT Live ID: 10509
Permanent link: https://videocast.nih.gov/launch.asp?17013

 

Podcast information
Audio Podcasts   Video Podcasts
  Description Runtime     Description Runtime
      Watch the podcast Audio Podcast 00:54:24
      Watch the podcast Video Podcast (CC) 00:54:24