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...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-06, Vol.279 (24), p.25567-25573
Main Authors: Makatsori, Dimitra, Kourmouli, Niki, Polioudaki, Hara, Shultz, Leonard D., Mclean, Kelvin, Theodoropoulos, Panayiotis A., Singh, Prim B., Georgatos, Spyros D.
Format: Article
Language:English
Subjects:
Animals
HeLa Cells
Heterochromatin - chemistry
Humans
Lamin B Receptor
Mass Spectrometry
Nuclear Envelope - chemistry
Receptors, Cytoplasmic and Nuclear - chemistry
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M313606200