ArticleJournal of cell science2014
The molecular basis of emerin-emerin and emerin-BAF interactions.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
49 citing papers in PubMed, 62 citations in OpenAlex.
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- X-linked Emery-Dreifuss muscular dystrophy: a multicenter, Italian, cohort study.Journal of neurology · 2026Article
- Nuclear Mechanics and Nuclear Mechanotransduction in Cancer Cell Migration and Invasion.Biomolecules · 2026Review
- Hierarchical membrane-chromatin tethering buffers nuclear envelope assembly against alterations in lipid flux.bioRxiv : the preprint server for biology · 2026Article
- A-type lamins anchor emerin at the inner nuclear membrane via two independent binding sites.The Journal of biological chemistry · 2026Article
- Barrier-to-Autointegration Factor 1: a key regulator of nuclear envelope integrity, genome stability, and disease progression.Frontiers in immunology · 2026Review
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
- The nuclear envelope and nuclear pore complexes in neurodegenerative diseases.Frontiers in cell and developmental biology · 2025Review
- Emerin mislocalization during chromatin bridge resolution can drive prostate cancer cell invasiveness in a collagen-rich microenvironment.Experimental & molecular medicine · 2024Article
- Review
- Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly inOpen biology · 2023Article
- Nuclear mechanosignaling in striated muscle diseases.Frontiers in physiology · 2023Review
- Native lamin A/C proteomes and novel partners from heart and skeletal muscle in a mouse chronic inflammation model of human frailty.Frontiers in cell and developmental biology · 2023Article
- Emerin prevents BAF-mediated aggregation of lamin A on chromosomes in telophase to allow nuclear membrane expansion and nuclear lamina formation.Molecular biology of the cell · 2022Article
- Collective analysis of the expression and prognosis for LEM-domain proteins in prostate cancer.World journal of surgical oncology · 2022Article
- Emerin self-assembly and nucleoskeletal coupling regulate nuclear envelope mechanics against stress.Journal of cell science · 2022Article
- The Role of Emerin in Cancer Progression and Metastasis.International journal of molecular sciences · 2021Review
- Article
- Genomic Action of Sigma-1 Receptor Chaperone Relates to Neuropathic Pain.Molecular neurobiology · 2021Article
- Di-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Emerin is a conserved membrane component of nuclear lamina structure. Here, we report an advance in understanding the molecular basis of emerin function: intermolecular emerin-emerin association. There were two modes: one mediated by association of residues 170-220 in one emerin molecule to residues 170-220 in another, and the second involving residues 170-220 and 1-132. Deletion analysis showed residues 187-220 contain a positive element essential for intermolecular association in cells. By contrast, deletion of residues 168-186 inactivated a proposed negative element, required to limit or control association. Association of GFP-emerin with nuclear BAF in cells required the LEM domain (residues 1-47) and the positive element. Emerin peptide arrays revealed direct binding of residues 170-220 to residues 206-225 (the proposed positive element), residues 147-174 (particularly P(153)MYGRDSAYQSITHYRP(169)) and the LEM domain. Emerin residues 1-132 and 159-220 were each sufficient to bind lamin A or B1 tails in vitro, identifying two independent regions of molecular contact with lamins. These results, and predicted emerin intrinsic disorder, support the hypothesis that there are multiple 'backbone' and LEM-domain configurations in a proposed intermolecular emerin network at the nuclear envelope.
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Registered trials
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.