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) |