The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope

Dimitra Makatsori, Niki Kourmouli, Hara Polioudaki, Leonard D Shultz, Kelvin McLean, Panayiotis A Theodoropoulos, Prim B Singh, Spyros D Georgatos

Research output: Contribution to journalArticle

105 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)25567-73
Number of pages7
JournalJournal of Biological Chemistry
Volume279
Issue number24
DOIs
Publication statusPublished - Jun 11 2004

Keywords

  • Animals
  • HeLa Cells
  • Heterochromatin
  • Humans
  • Mass Spectrometry
  • Nuclear Envelope
  • Receptors, Cytoplasmic and Nuclear
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

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    Makatsori, D., Kourmouli, N., Polioudaki, H., Shultz, L. D., McLean, K., Theodoropoulos, P. A., Singh, P. B., & Georgatos, S. D. (2004). The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope. Journal of Biological Chemistry, 279(24), 25567-73. https://doi.org/10.1074/jbc.M313606200