The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope.
Heterochromatin, Human, Nuclear-Envelope, Receptors-Cytoplasmic-and-Nuclear, Spectrum-Analysis-Mass
J Biol Chem 2004 Jun; 279(24):25567-73.
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.
Makatsori, D; Kourmouli, N; Polioudaki, H; Shultz, L D.; McLean, K; Theodoropoulos, P A.; Singh, P B.; and Georgatos, S D., " The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope." (2004). Faculty Research 2000 - 2009. 781.