The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope.
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
Dimitra
D
Laboratory of Biology, The University of Ioannina, School of Medicine, 45 110 Ioannina, Greece.
Kourmouli
Niki
N
Polioudaki
Hara
H
Shultz
Leonard D
LD
McLean
Kelvin
K
Theodoropoulos
Panayiotis A
PA
Singh
Prim B
PB
Georgatos
Spyros D
SD
D000818:Animals; D006367:HeLa Cells; D006570:Heterochromatin / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry; D009685:Nuclear Envelope / Q000737:chemistry*; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D000097682:Lamin B Receptor
D006570:Heterochromatin; D018160:Receptors, Cytoplasmic and Nuclear; D000097682:Lamin B Receptor