Dataset Information


Acetylation of p65 at lysine 314 is important for late NF-kappaB-dependent gene expression.

ABSTRACT: BACKGROUND: NF-kappaB regulates the expression of a large number of target genes involved in the immune and inflammatory response, apoptosis, cell proliferation, differentiation and survival. We have earlier reported that p65, a subunit of NF-kappaB, is acetylated in vitro and in vivo at three different lysines (K310, K314 and K315) by the histone acetyltransferase p300. RESULTS: In this study, we describe that site-specific mutation of p65 at lysines 314 and 315 enhances gene expression of a subset of NF-kappaB target genes including Mmp10 and Mmp13. Increased gene expression was mainly observed three hours after TNFalpha stimulation. Chromatin immunoprecipitation (ChIP) experiments with an antibody raised against acetylated lysine 314 revealed that chromatin-bound p65 is indeed acetylated at lysine 314. CONCLUSIONS: Together, our results establish acetylation of K314 as an important regulatory modification of p65 and subsequently of NF-kappaB-dependent gene expression.

SUBMITTER: Rothgiesser KM 

PROVIDER: S-EPMC2823688 | BioStudies | 2010-01-01

REPOSITORIES: biostudies

Similar Datasets

2010-01-10 | GSE15196 | GEO
2010-01-10 | GSE15196 | GEO
2010-04-08 | E-GEOD-15196 | ArrayExpress
1000-01-01 | S-EPMC2275151 | BioStudies
1000-01-01 | S-EPMC1636810 | BioStudies
2017-01-01 | S-EPMC5628277 | BioStudies
1000-01-01 | S-EPMC2573235 | BioStudies
2018-10-19 | PXD001932 | Pride
2009-01-01 | S-EPMC2760979 | BioStudies
2008-01-01 | S-EPMC2680745 | BioStudies