ArticleThe Journal of biological chemistry2012
Solution structure and molecular interactions of lamin B receptor Tudor domain.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- The role of electrostatic interactions in the phase separation of HP1α and its protein binding partners.bioRxiv : the preprint server for biology · 2026Article
- The nuclear periphery confers repression on H3K9me2-marked genes and transposons to shape cell fate.Nature cell biology · 2025Article
- Neutrophils secrete exosome-associated DNA to resolve sterile acute inflammation.Nature cell biology · 2025Article
- Analysis of the interplay between MeCP2 and histone H1 duringEpigenetics · 2023Article
- Characterization of lamin B receptor of Sf9 cells and its fate during Autographa californica nucleopolyhedrovirus infection.Cytotechnology · 2020Article
- Twin enzymes, divergent control: The cholesterogenic enzymes DHCR14 and LBR are differentially regulated transcriptionally and post-translationally.The Journal of biological chemistry · 2020Article
- Review
- Article
- ELYS regulates the localization of LBR by modulating its phosphorylation state.Journal of cell science · 2016Article
- Histones and histone modifications in perinuclear chromatin anchoring: from yeast to man.EMBO reports · 2016Review
- ELCS in ice: cryo-electron microscopy of nuclear envelope-limited chromatin sheets.Chromosoma · 2014Article
- Tudor: a versatile family of histone methylation 'readers'.Trends in biochemical sciences · 2013Review
- Lamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation.The Journal of biological chemistry · 2012Article
- Knock-down of methyl CpG-binding protein 2 (MeCP2) causes alterations in cell proliferation and nuclear lamins expression in mammalian cells.BMC cell biology · 2012Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lamin B receptor (LBR) is a polytopic protein of the nuclear envelope thought to connect the inner nuclear membrane with the underlying nuclear lamina and peripheral heterochromatin. To better understand the function of this protein, we have examined in detail its nucleoplasmic region, which is predicted to harbor a Tudor domain (LBR-TD). Structural analysis by multidimensional NMR spectroscopy establishes that LBR-TD indeed adopts a classical β-barrel Tudor fold in solution, which, however, features an incomplete aromatic cage. Removal of LBR-TD renders LBR more mobile at the plane of the nuclear envelope, but the isolated module does not bind to nuclear lamins, heterochromatin proteins (MeCP2), and nucleosomes, nor does it associate with methylated Arg/Lys residues through its aromatic cage. Instead, LBR-TD exhibits tight and stoichiometric binding to the "histone-fold" region of unassembled, free histone H3, suggesting an interesting role in histone assembly. Consistent with such a role, robust binding to native nucleosomes is observed when LBR-TD is extended toward its carboxyl terminus, to include an area rich in Ser-Arg residues. The Ser-Arg region, alone or in combination with LBR-TD, binds both unassembled and assembled H3/H4 histones, suggesting that the TD/RS interface may operate as a "histone chaperone-like platform."
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.