RRC ID 44135
著者 Hirano Y, Hizume K, Kimura H, Takeyasu K, Haraguchi T, Hiraoka Y.
タイトル Lamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation.
ジャーナル J Biol Chem
Abstract Inner nuclear membrane proteins provide a structural framework for chromatin, modulating transcription beneath the nuclear envelope. Lamin B receptor (LBR) is a classical inner nuclear membrane protein that associates with heterochromatin, and its mutations are known to cause Pelger-Huët anomaly in humans. However, the mechanisms by which LBR organizes heterochromatin remain to be elucidated. Here, we show that LBR represses transcription by binding to chromatin regions that are marked by specific histone modifications. The tudor domain (residues 1-62) of LBR primarily recognizes histone H4 lysine 20 dimethylation and is essential for chromatin compaction, whereas the whole nucleoplasmic region (residues 1-211) is required for transcriptional repression. We propose a model in which the nucleoplasmic domain of LBR tethers epigenetically marked chromatin to the nuclear envelope and transcriptional repressors are loaded onto the chromatin through their interaction with LBR.
巻・号 287(51)
ページ 42654-63
公開日 2012-12-14
DOI 10.1074/jbc.M112.397950
PII S0021-9258(20)43758-5
PMID 23100253
PMC PMC3522266
MeSH Amino Acid Sequence HEK293 Cells HeLa Cells Heterochromatin / metabolism* Histones / metabolism* Humans Lamin Type B / metabolism Lysine / metabolism Methylation Models, Biological Molecular Sequence Data Nuclear Envelope / metabolism Protein Binding Protein Multimerization Protein Processing, Post-Translational* Protein Structure, Tertiary Receptors, Cytoplasmic and Nuclear / chemistry Receptors, Cytoplasmic and Nuclear / metabolism* Repressor Proteins / metabolism Transcription, Genetic
IF 4.238
引用数 63
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
ヒト・動物細胞 HeLa(RCB0007)