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Updated: Aug 25, 2026

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
Published on: January 17, 2025
The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked
Dimitra Makatsori1, Niki Kourmouli, Hara Polioudaki
1Laboratory of Biology, The University of Ioannina, School of Medicine, 45 110 Ioannina, Greece.
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.
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