ArticleJournal of cell science2012
The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 64 citations in OpenAlex.
- The ultrafine-bridge-associated endonuclease ANKLE1 is stimulated by tension in DNA to process branch-points.Nucleic acids research · 2026Article
- Sequence and structural alignments reveal insights into ANKLE2 evolution and function.Protein science : a publication of the Protein Society · 2026Article
- Nuclear envelope proteins in cancer: revisiting the significance of LEM-domain proteins.Frontiers in cell and developmental biology · 2026Review
- Barrier-to-Autointegration Factor 1: a key regulator of nuclear envelope integrity, genome stability, and disease progression.Frontiers in immunology · 2026Review
- ANKLE1 processes chromatin bridges by cleaving mechanically stressed DNA.Nature communications · 2025Article
- 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
- Long noncoding RNAs and metabolic memory associated with continued progression of diabetic retinopathy.Journal of diabetes · 2024Article
- Formation and resolution of meiotic chromosome entanglements and interlocks.Journal of cell science · 2024Review
- Molecular functions of ANKLE2 and its implications in human disease.Disease models & mechanisms · 2024Review
- Biochemical and mechanistic analysis of the cleavage of branched DNA by human ANKLE1.Nucleic acids research · 2023Article
- Human Endonuclease ANKLE1 Localizes at the Midbody and Processes Chromatin Bridges to Prevent DNA Damage and cGAS-STING Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- ANKLE1 cleaves mitochondrial DNA and contributes to cancer risk by promoting apoptosis resistance and metabolic dysregulation.Communications biology · 2023Article
- Characterization of a prognostic model for lung squamous cell carcinoma based on eight stemness index-related genes.BMC pulmonary medicine · 2022Article
- Collective analysis of the expression and prognosis for LEM-domain proteins in prostate cancer.World journal of surgical oncology · 2022Article
- Review
- Investigation of triple-negative breast cancer risk alleles in an International African-enriched cohort.Scientific reports · 2021Article
- Coordinated roles of SLX4 and MutSβ in DNA repair and the maintenance of genome stability.Critical reviews in biochemistry and molecular biology · 2021Review
- The Last Chance Saloon.Frontiers in cell and developmental biology · 2021Review
- The Relationship Between Microbiomes and Selective Regimes in the Sponge GenusFrontiers in microbiology · 2021Article
- Human ANKLE1 Is a Nuclease Specific for Branched DNA.Journal of molecular biology · 2020Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) defines a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF). Here, we describe a LEM protein annotated in databases as 'Ankyrin repeat and LEM domain-containing protein 1' (Ankle1). We show that Ankle1 is conserved in metazoans and contains a unique C-terminal GIY-YIG motif that confers endonuclease activity in vitro and in vivo. In mammals, Ankle1 is predominantly expressed in hematopoietic tissues. Although most characterized LEM proteins are components of the inner nuclear membrane, ectopic Ankle1 shuttles between cytoplasm and nucleus. Ankle1 enriched in the nucleoplasm induces DNA cleavage and DNA damage response. This activity requires both the catalytic C-terminal GIY-YIG domain and the LEM motif, which binds chromatin via BAF. Hence, Ankle1 is an unusual LEM protein with a GIY-YIG-type endonuclease activity in higher eukaryotes.
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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.