The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope.
Document Type
Article
Publication Date
2004
Keywords
Heterochromatin, Human, Nuclear-Envelope, Receptors-Cytoplasmic-and-Nuclear, Spectrum-Analysis-Mass
First Page
25567
Last Page
25573
JAX Source
J Biol Chem 2004 Jun; 279(24):25567-73.
Abstract
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.
Recommended Citation
Makatsori D,
Kourmouli N,
Polioudaki H,
Shultz LD,
McLean K,
Theodoropoulos PA,
Singh PB,
Georgatos SD.
The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope. J Biol Chem 2004 Jun; 279(24):25567-73.