Skip Navigation

Cardiovascular Research 2007 75(2):229-239; doi:10.1016/j.cardiores.2007.04.013
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Raines, K. W.
Right arrow Articles by Campbell, S. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Raines, K. W.
Right arrow Articles by Campbell, S. L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Copyright © 2007, European Society of Cardiology

Nitric oxide cell signaling: S-nitrosation of Ras superfamily GTPases

Kimberly W. Rainesa,b, Marcelo G. Boninic and Sharon L. Campbella,b,*

aDepartment of Biochemistry and Biophysics, University of North Carolina, 530 Mary Ellen Jones Building, Chapel Hill, NC 27599-7260, United States
bLineberger Comprehensive Cancer Center, University of North Carolina, 530 Mary Ellen Jones Building, Chapel Hill, NC 27599-7260, United States
cLaboratory of Pharmacology and Chemistry, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, United States

* Corresponding author. Lineberger Comprehensive Cancer Center, University of North Carolina, 530 Mary Ellen Jones Building, Chapel Hill, NC 27599-7260, United States. Tel.: +1 919 966 7139; fax: +1 919 966 2852. campbesl{at}med.unc.edu

The Ras superfamily of small GTPases cycle between inactive GDP-bound and active GTP-bound states to modulate a diverse array of processes involved in cellular growth control. While the basic mechanisms by which GTPase regulatory proteins regulate GTPase substrates have been revealed through numerous studies, detailed studies into the mechanism(s) of free radical-mediated GTPase regulation have only more recently been tackled. This article reviews the mechanism of free radical-mediated GTPase regulation and shows nitric oxide can serve as important regulator of small GTPase proteins (i.e. Ras and RhoA) through protein modifications such as S-nitrosation.

KEYWORDS Nitric oxide; Redox signaling; Small GTPases


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
 Proc. Natl. Acad. Sci. USAHome page
S. Ibiza, A. Perez-Rodriguez, A. Ortega, A. Martinez-Ruiz, O. Barreiro, C. A. Garcia-Dominguez, V. M. Victor, J. V. Esplugues, J. M. Rojas, F. Sanchez-Madrid, et al.
Endothelial nitric oxide synthase regulates N-Ras activation on the Golgi complex of antigen-stimulated T cells
PNAS, July 29, 2008; 105(30): 10507 - 10512.
[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.