The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope

被引:122
作者
Makatsori, D
Kourmouli, N
Polioudaki, H
Shultz, LD
Mclean, K
Theodoropoulos, PA
Singh, PB
Georgatos, SD [1 ]
机构
[1] Univ Ioannina, Sch Med, Biol Lab, GR-45110 Ioannina, Greece
[2] Roslin Inst, Dept Gene Express & Dev, Nucl Reprogramming Lab, Roslin EH25 9PS, Midlothian, Scotland
[3] Univ Crete, Sch Med, Dept Basic Sci, Iraklion 95110, Crete, Greece
[4] Jackson Lab, Bar Harbor, ME 04609 USA
[5] Moredun Res Inst, Funct Genom Unit, Penicuik EH26 0PZ, Midlothian, Scotland
关键词
D O I
10.1074/jbc.M313606200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using heterochromatin-enriched fractions, we have detected specific binding of mononucleosomes to the N-terminal domain of the inner nuclear membrane protein lamin B receptor. Mass spectrometric analysis reveals that LBR-associated particles contain complex patterns of methylated/acetylated histones and are devoid of "euchromatic" epigenetic marks. LBR binds heterochromatin as a higher oligomer and forms distinct nuclear envelope microdomains in vivo. The organization of these membrane assemblies is affected significantly in heterozygous ic (ichthyosis) mutants, resulting in a variety of structural abnormalities and nuclear defects.
引用
收藏
页码:25567 / 25573
页数:7
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