ArticleThe EMBO journal2001
LAP2 binds to BAF.DNA complexes: requirement for the LEM domain and modulation by variable regions.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 207 citations in OpenAlex.
- Sequence and structural alignments reveal insights into ANKLE2 evolution and function.Protein science : a publication of the Protein Society · 2026Article
- LEM-Domain-Containing Inner Nuclear Membrane Proteins: Emerging Regulators of Intranuclear Signaling.International journal of molecular sciences · 2026Review
- A novel antiviral role of ankyrin repeat and LEM domain-containing 2 (ANKLE2) in restricting vaccinia virus through barrier to autointegration factor (BAF).Journal of virology · 2025Article
- Mitotic dynamics of the nuclear lamina in the backstage of chromosome separation.Communications biology · 2025Review
- Functional dissection of the conserved C. elegans LEM-3/ANKLE1 nuclease reveals a crucial requirement for the LEM-like and GIY-YIG domains for DNA bridge processing.Nucleic acids research · 2025Article
- An interkinetic envelope surrounds chromosomes between meiosis I and II in C. elegans oocytes.The Journal of cell biology · 2025Article
- Crosstalk between mitotic reassembly and repair of the nuclear envelope.Nucleus (Austin, Tex.) · 2024Review
- An interkinetic envelope surrounds chromosomes between meiosis I and II inbioRxiv : the preprint server for biology · 2024Article
- Lamin chromatin binding is modulated by interactions of different LAP2α domains with lamins and chromatin.iScience · 2024Article
- Molecular functions of ANKLE2 and its implications in human disease.Disease models & mechanisms · 2024Review
- A genome-wide RNAi screen for genes important for proliferation of cultured Drosophila cells at low temperature identifies the Ball/VRK protein kinase.Chromosoma · 2023Article
- MALL, a membrane-tetra-spanning proteolipid overexpressed in cancer, is present in membraneless nuclear biomolecular condensates.Cellular and molecular life sciences : CMLS · 2022Article
- LAP2α preserves genome integrity through assisting RPA deposition on damaged chromatin.Genome biology · 2022Article
- The Nuclear Lamina.Cold Spring Harbor perspectives in biology · 2022Review
- Transfected plasmid DNA is incorporated into the nucleus via nuclear envelope reformation at telophase.Communications biology · 2022Article
- Effects of forces on chromatin.APL bioengineering · 2021Review
- The Role of Emerin in Cancer Progression and Metastasis.International journal of molecular sciences · 2021Review
- Di-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners.Nucleic acids research · 2021Article
- Barrier-to-autointegration-factor (Banf1) modulates DNA double-strand break repair pathway choice via regulation of DNA-dependent kinase (DNA-PK) activity.Nucleic acids research · 2021Article
- SATB2-LEMD2 interaction links nuclear shape plasticity to regulation of cognition-related genes.The EMBO journal · 2021Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
LAP2 belongs to a family of nuclear membrane proteins sharing a 43 residue LEM domain. All LAP2 isoforms have the same N-terminal 'constant' region (LAP2-c), which includes the LEM domain, plus a C-terminal 'variable' region. LAP2-c polypeptide inhibits nuclear assembly in Xenopus extracts, and binds in vitro to barrier-to-autointegration factor (BAF), a DNA-bridging protein. We tested 17 Xenopus LAP2-c mutants for nuclear assembly inhibition, and binding to BAF and BAF small middle dotDNA complexes. LEM domain mutations disrupted all activities tested. Some mutations outside the LEM domain had no effect on binding to BAF, but disrupted activity in Xenopus extracts, suggesting that LAP2-c has an additional unknown function required to inhibit nuclear assembly. Mutagenesis results suggest that BAF changes conformation when complexed with DNA. The binding affinity of LAP2 was higher for BAF small middle dotDNA complexes than for BAF, suggesting that these interactions are physiologically relevant. Nucleoplasmic domains of Xenopus LAP2 isoforms varied 9-fold in their affinities for BAF, but all isoforms supershifted BAF small middle dotDNA complexes. We propose that the LEM domain is a core BAF-binding domain that can be modulated by the variable regions of LAP2 isoforms.
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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.