HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: fj.07-101816v1 22/7/2285    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Liu, G. Articles by Abraham, E. Search for Related Content PubMed PubMed Citation Articles by Liu, G. Articles by Abraham, E.

Interleukin-1 receptor-associated kinase (IRAK) -1-mediated NF-B activation requires cytosolic and nuclear activity

Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, USA

¹Correspondence: Department of Medicine, University of Alabama at Birmingham School of Medicine, 420 Boshell Bldg., 1808 7th Ave., South, Birmingham, AL 35294, USA. E-mail: eabraham{at}uab.edu

Interleukin-1 receptor-associated kinase (IRAK) -1 plays an essential role in Toll-like receptor/interleukin-1 receptor (TLR/IL-1R) -associated NF-B activation through its involvement in IKK activation, which then leads to subsequent IB degradation and NF-B nuclear translocation. In the present studies, we demonstrate a novel pathway in which IRAK-1 present in the nucleus participates in NF-B-dependent gene expression. Nuclear localization of IRAK-1 is increased on cellular stimulation with IL-1 and LPS, or CRM-1-dependent nuclear export blockade. Induction of IRAK-1 produces enhanced NF-B transcriptional activity that precedes IB- degradation and nuclear translocation of NF-B. IRAK-1 binds to the promoter of NF-B-regulated gene, IB-, and enhances binding of the NF-B p65 subunit to NF-B responsive elements within the IB- promoter. IRAK-1 phosphorylates histone H3 in vitro and is required for IL-1-induced phosphorylation of histone H3 at serine 10 in vivo. These data indicate that both cytosolic and nuclear actions of IRAK-1 participate in the activation of NF-B-dependent transcriptional events.—Liu, G., Park, Y.-J., Abraham, E. Interleukin-1 receptor-associated kinase (IRAK) -1-mediated NF-B activation requires cytosolic and nuclear activity.

Key Words: transcription • histone H3 • nuclear translocation • Toll-like receptor

This article has been cited by other articles:

				G. Liu, Y.-J. Park, Y. Tsuruta, E. Lorne, and E. Abraham p53 Attenuates Lipopolysaccharide-Induced NF-{kappa}B Activation and Acute Lung Injury J. Immunol., April 15, 2009; 182(8): 5063 - 5071. [Abstract] [Full Text] [PDF]

				W. Song, G. Liu, C. A. Bosworth, J. R. Walker, G. A. Megaw, A. Lazrak, E. Abraham, W. M. Sullender, and S. Matalon Respiratory Syncytial Virus Inhibits Lung Epithelial Na+ Channels by Up-regulating Inducible Nitric-oxide Synthase J. Biol. Chem., March 13, 2009; 284(11): 7294 - 7306. [Abstract] [Full Text] [PDF]