Nucleic Acids Research Advance Access originally published online on December 14, 2006
Nucleic Acids Research 2007 35(2):517-528; doi:10.1093/nar/gkl1080
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Nucleic Acids Research, 2007, Vol. 35, No. 2 517-528
© 2006 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Glucocorticoid-induced leucine zipper (GILZ)/NF-
B interaction: role of GILZ homo-dimerization and C-terminal domain
1 Department of Clinical and Experimental Medicine IBiT Foundation, 06122 Perugia, Italy 2 Department of Drug Chemistry and Technology, University of Perugia IBiT Foundation, 06122 Perugia, Italy 3 Polo Scientifico e Didattico di Terni, 05100 Terni Italy
*To whom correspondence should be addressed at Department of Clinical and Experimental Medicine, Section of Pharmacology, Via del Giochetto, 06100 Perugia, Italy. Tel: +39 075 585 7467; Fax: +39 075 585 7405; Email: riccardi{at}unipg.it
Received August 24, 2006. Revised October 28, 2006. Accepted November 16, 2006.
Glucocorticoid-induced leucine zipper (GILZ) is a 137 amino acid protein, rapidly induced by treatment with glucocorticoids (GC), characterized by a leucine zipper (LZ) domain (76–97 amino acids), an N-terminal domain (1–75 amino acids) and a C-terminal PER domain (98–137 amino acids) rich in proline and glutamic acid residues. We have previously shown that GILZ binds to and inhibits NF-
B activity. In the present study we used a number of mutants with the aim of defining the GILZ molecular domains responsible for GILZ/p65NF-B interaction. Results, obtained by in vitro and in vivo co-immunoprecipitation (Co-IP) and by transcriptional activity experiments, indicate that GILZ homo-dimerization, through the LZ domain, as well as the C-terminal PER domain, particularly the 121–123 amino acids, are both necessary for GILZ interaction with NF-B, inhibition of transcriptional activity and of IL-2 synthesis.
The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  K. De Bosscher and G. Haegeman Minireview: Latest Perspectives on Antiinflammatory Actions of Glucocorticoids Mol. Endocrinol., March 1, 2009; 23(3): 281 - 291. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Cuzzocrea, S. Bruscoli, E. Mazzon, C. Crisafulli, V. Donato, R. Di Paola, E. Velardi, E. Esposito, G. Nocentini, and C. Riccardi Peroxisome Proliferator-Activated Receptor-{alpha} Contributes to the Anti-Inflammatory Activity of Glucocorticoids Mol. Pharmacol., February 1, 2008; 73(2): 323 - 337. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Soundararajan, J. Wang, D. Melters, and D. Pearce Differential Activities of Glucocorticoid-induced Leucine Zipper Protein Isoforms J. Biol. Chem., December 14, 2007; 282(50): 36303 - 36313. [Abstract] [Full Text] [PDF]
|
|