Abstract
We recently reported that a large proportion of aggressive squamous cell carcinomas of humans and mice express markedly reduced IKKalpha. However, the role of IKKalpha in maintaining genomic stability is unknown. Here we reported that IKKalpha-deficient keratinocytes had a defect in the G(2)/M cell-cycle arrest in response to DNA damage due to downregulated 14-3-3sigma, a cell cycle checkpoint protein. Trimethylated histone H3 lysine 9 (H3-K9) was found to associate with the histone trimethyltransferase Suv39h1 and DNA methyltransferase Dnmt3a in the methylated 14-3-3sigma locus. Reintroduction of IKKalpha restored the expression of 14-3-3sigma. IKKalpha was found to associate with H3 in 14-3-3sigma, which prevented access of Suv39h1 to H3, thereby preventing hypermethylation of 14-3-3sigma. IKKalpha mutants that failed to bind to H3 did not restore the expression of 14-3-3sigma. Thus, IKKalpha protects the 14-3-3sigma locus from hypermethylation, which serves as a mechanism of maintaining genomic stability in keratinocytes.
MeSH Terms
14-3-3 Proteins/genetics
Animals
Base Sequence
Carcinoma, Squamous Cell/genetics,metabolism
Cell Division/genetics
Cells, Cultured
CpG Islands
DNA (Cytosine-5-)-Methyltransferases/metabolism
DNA Methylation
DNA Methyltransferase 3A
DNA Primers/genetics
Down-Regulation
G2 Phase/genetics
Gene Silencing
Genomic Instability
Histones/metabolism
Humans
I-kappa B Kinase/deficiency,genetics,metabolism
Keratinocytes/cytology,metabolism
Methyltransferases/metabolism
Mice
Molecular Sequence Data
Mutation
Repressor Proteins/metabolism
Skin Neoplasms/genetics,metabolism
Chemicals
14-3-3 Proteins
DNA Primers
DNMT3A protein, human
Dnmt3a protein, mouse
Histones
Repressor Proteins
Sfn protein, mouse
Suv39h1 protein, mouse
Methyltransferases
DNA (Cytosine-5-)-Methyltransferases
DNA Methyltransferase 3A
Chuk protein, mouse
I-kappa B Kinase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Zhu Feng
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Xia Xiaojun
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Liu Bigang
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Shen Jianjun
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Hu Yuhui
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Person Maria
Division of Pharmacology and Toxicology, College of Pharmacy, The University of Texas at Austin, Austin, TX 78712, USA.
Hu Yinling
Science Park Research Division, The University of Texas M.D. Anderson Cancer Center, Smithville, TX 78957, USA. Electronic address: yhu@mdanderson.org.