The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope
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Authors
Makatsori, D.
Kourmouli, N.
Polioudaki, H.
Shultz, L. D.
McLean, K.
Theodoropoulos, P. A.
Singh, P. B.
Georgatos, S. D.
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peer-reviewed
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J Biol Chem
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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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Animals, HeLa Cells, Heterochromatin/*chemistry, Humans, Mass Spectrometry, Nuclear Envelope/*chemistry, Receptors, Cytoplasmic and Nuclear/*chemistry
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http://www.ncbi.nlm.nih.gov/pubmed/15056654
http://www.jbc.org/content/279/24/25567.full.pdf
http://www.jbc.org/content/279/24/25567.full.pdf
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en
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Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής