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
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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
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