Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print May 30, 2007
Mol. Biol. Cell 10.1091/mbc.E06-09-0869

A more recent version of this article appeared on August 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E06-09-0869v1
18/8/3015    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bartz, R.
Right arrow Articles by Liu, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bartz, R.
Right arrow Articles by Liu, P.

Submitted on September 27, 2006
Revised on May 7, 2007
Accepted on May 17, 2007

Evidence that Mono-ADP-Ribosylation of CtBP1/BARS Regulates Lipid Storage

René Bartz,* Joachim Seemann,* John K. Zehmer,* Ginette Serrero,{dagger} Kent D. Chapman,{ddagger} Richard G.W. Anderson,* and Pingsheng Liu*

*Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039; {dagger}A&G Pharmaceutical Inc., Columbia, MD 21045; {ddagger}Department of Biological Sciences, University of North Texas, Denton, TX 76203

Monitoring Editor: Vivek Malhotra

Mono-ADP-ribosylation is emerging as an important post-translational modification that modulates a variety of cell signaling pathways. Here we present evidence that mono-ADP-ribosylation of the transcriptional corepressor CtBP1/BARS regulates neutral lipid storage in droplets that are surrounded by a monolayer of phospholipid and associated proteins. CtBP1/BARS is a NAD binding protein that becomes ribosylated when cells are exposed to Brefeldin A (BFA). Both endogenous lipid droplets and droplets enlarged by oleate treatment are lost after 12 h exposure to BFA. Lipid loss requires new protein synthesis and is blocked by multiple ribosylation inhibitors but is not stimulated by disruption of the Golgi apparatus or the ER unfolded protein response. siRNA knockdown of CtBP1/BARS mimics the effect of BFA, and mouse embryonic fibroblasts derived from embryos that are deficient in CtBP1/BARS appear to be defective in lipid accumulation. We conclude that mono-ADP-ribosylation of CtBP1/BARS inactivates its repressor function, which leads to the activation of genes that regulate neutral lipid storage.

Address correspondence to: Richard G.W. Anderson (richard.anderson{at}utsouthwestern.edu)




This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
N. Sue, B. H. A. Jack, S. A. Eaton, R. C. M. Pearson, A. P. W. Funnell, J. Turner, R. Czolij, G. Denyer, S. Bao, J. C. Molero-Navajas, et al.
Targeted Disruption of the Basic Kruppel-Like Factor Gene (Klf3) Reveals a Role in Adipogenesis
Mol. Cell. Biol., June 15, 2008; 28(12): 3967 - 3978.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.