Skip Navigation


Glycobiology Advance Access originally published online on February 27, 2006
Glycobiology 2006 16(6):551-563; doi:10.1093/glycob/cwj096
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplemental Data
Right arrow All Versions of this Article:
16/6/551    most recent
cwj096v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Whisenhunt, T. R.
Right arrow Articles by Kudlow, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Whisenhunt, T. R.
Right arrow Articles by Kudlow, J. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development

Thomas R. Whisenhunt2,3, Xiaoyong Yang6, Damon B. Bowe4, Andrew J. Paterson5, Brian A. Van Tine3 and Jeffrey E. Kudlow1,2,4,5

2 Department of Cell Biology, 3 Medical Scientist Training Program, 4 Department of Pharmacology and Toxicology, and 5 Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294; and 6Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037

1 To whom correspondence should be addressed; e-mail: kudlow{at}uab.edu

Received on January 18, 2006; revised on February 14, 2006; accepted on February 21, 2006

Although the knowledge that nuclear and cytoplasmic proteins are modified with N-acetylglucosamine has existed for decades, little has been shown as to its function until recently. There are now substantial data highlighting the significance of proper regulation of this modification in multiple cellular processes. Currently, only two enzymes are known that regulate this modification. O-GlcNAc transferase (OGT) modifies protein substrates posttranslationally by adding the N-acetylglucosamine. Bifunctional nuclear/cytoplasmic O-GlcNAcase and acetyl transferase (NCOAT) is responsible for cleaving the modification from target proteins. Here, we demonstrate for the first time an unusual association of these two opposing enzymes into a single O-GlcNAczyme complex. NCOAT and OGT associate strongly through specific domains such that NCOAT accompanies OGT, with histone deacetylases (HDACs), into transcription corepression complexes. Exclusion of NCOAT activities from OGT association blocks proper estrogen-dependent cell signaling as well as mammary development in transgenic mice. This demonstrates that NCOAT is in a strategic position to rapidly counteract OGT and HDAC without requiring its recruitment.

Key words: corepressor / estrogen / HAT / O-GlcNAcase / OGT


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
R. J. Copeland, J. W. Bullen, and G. W. Hart
Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity
Am J Physiol Endocrinol Metab, July 1, 2008; 295(1): E17 - E28.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
K. A. Robinson, L. E. Ball, and M. G. Buse
Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes
Am J Physiol Endocrinol Metab, March 1, 2007; 292(3): E884 - E890.
[Abstract] [Full Text] [PDF]

Home page
 Cardiovasc ResHome page
N. Fulop, R. B. Marchase, and J. C. Chatham
Role of protein O-linked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system
Cardiovasc Res, January 15, 2007; 73(2): 288 - 297.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
D. B. Bowe, A. Sadlonova, C. A. Toleman, Z. Novak, Y. Hu, P. Huang, S. Mukherjee, T. Whitsett, A. R. Frost, A. J. Paterson, et al.
O-GlcNAc Integrates the Proteasome and Transcriptome To Regulate Nuclear Hormone Receptors
Mol. Cell. Biol., November 15, 2006; 26(22): 8539 - 8550.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.