ANKLE1
- Known as:
- ANKLE1
- Catalog number:
- 001591A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ANKLE1
Related genes to: ANKLE1
- Gene:
- ANKLE1 NIH gene
- Name:
- ankyrin repeat and LEM domain containing 1
- Previous symbol:
- ANKRD41
- Synonyms:
- FLJ39369, LEMD6
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2005-05-29
- Date modifiied:
- 2016-04-25
Related products to: ANKLE1
Related articles to: ANKLE1
- Covalent linkages between chromosomes form naturally as a result of recombination or DNA replication. These can persist until late mitosis, resulting in the formation of ultrafine bridges, preventing cell division and causing genome instability through mechanical DNA rupture. The endonuclease ANKLE1, selective for DNA branchpoints during cytokinesis and localizing at the cell midbody, is ideally poised to act as the 'enzyme of last resort' in processing interchromosomal bridges, thereby allowing cell division. How ANKLE1 catalyzes DNA cleavage under the high tension that exists in interchromosomal bridges during mitosis remains unexplored. Using optical tweezers, we show that ANKLE1 is a mechanosensitive endonuclease whose catalytic activity is stimulated by tension in its DNA substrate. At high tension, we observe that the rate at which ANKLE1 catalyzes the cleavage of DNA junctions increases continuously with applied tension, with a 20-fold increase in the cleavage rate at 60 pN. This indicates that ANKLE1 has evolved to detect and respond to tension-induced changes to the DNA structure in a manner that facilitates nucleolytic activity. This mechanoenzymological response of ANKLE1 to tension within its DNA substrate reveals how this enzyme is well suited to its suggested biological role as an ultrafine-bridge processing enzyme during late mitosis. - Source: PubMed
Ray Korak KumarKaczmarczyk Artur PFreeman Alasdair D JLeow FaithWilson Timothy JRueda David SLilley David M J - Nuclear envelope dysfunction is increasingly recognized as a driver of cancer-associated alterations in chromatin organization, genome stability, and mechanotransduction. Among inner nuclear membrane components are the LEM-domain (LEM-D) proteins LAP2/TMPO, emerin (EMD), LEMD1, LEMD2, MAN1/LEMD3, ANKLE1, and ANKLE2. Accumulating evidence links dysregulation of these proteins to hallmark cancer processes, including cell-cycle control, epithelial-mesenchymal transition, genome instability, and therapeutic resistance. This review synthesizes recent mechanistic and translational findings on LEM-D proteins in cancer, highlighting isoform-specific functions, context-dependent oncogenic versus tumor-suppressive roles, and convergence on key pathways such as Wnt/β-catenin, PI3K/AKT, MAPK, and TGF-β signaling. Concrete evidence for prognostic value varies across the LEM-D proteins. While much of the current evidence derives from transcript-level and preclinical studies, emerging data suggest that LEM-D proteins contribute to nuclear stress adaptation and may represent context-dependent therapeutic vulnerabilities. We discuss their prognostic and predictive potential, critically evaluate limitations in current datasets, and present a unifying framework linking LEM-D dysfunction to genome instability, altered signalling, and therapy resistance. Thus, despite growing evidence of therapeutic potential, these proteins are better positioned as biomarkers to guide current therapies. - Source: PubMed
Publication date: 2026/04/22
Jobe AmieMirza SameerVijayan Ranjit - Compared to European American women, African American women are more likely to be diagnosed with triple-negative breast cancer (TNBC). This difference may be partially due to genetic factors. This study aims to investigate associations of African ancestry and risk variants with TNBC among African American women. - Source: PubMed
Publication date: 2026/05/07
Jia GuochongLiu LiliPing JieFiorica Peter NGuo XingyiTao RanLi BingshanGu JianJohn Esther MOlopade Olufunmilayo IPress Michael FBrewster Abenaa MOlshan Andrew FZirpoli GaryButler Ebonee NHuang MaoshengHuo DezhengPalmer Julie RHaiman Christopher AAmbrosone Christine BTroester Melissa ALong JirongYao SongZheng Wei - This study was designed to identify genes for further study as modifiers of the severity of cardiomyopathy in DMD-related Duchenne Muscular Dystrophy (DMD). - Source: PubMed
Publication date: 2026/01/07
Geddes Gabrielle CWare Stephanie MSchwantes-An Tae-HwiAbreu Marco AParent John JEarl Conner CSoslow Jonathan HMarkham Larry W - Chromatin bridges experience significant tension due to spindle fiber pulling and cell migration. Uncontrolled breakage of chromatin bridges by actomyosin contractile forces leads to detrimental consequences. The existence of specialized mechanisms that process chromatin bridges to prevent catastrophic rupture remains uncertain. Here, we uncover a unique property of ANKLE1, a midbody-tethered endonuclease implicated in chromatin bridge processing, in sensing and responding to DNA tension and supercoiling during cell division. Using single-molecule analyses, we found that ANKLE1 specifically cuts supercoiled or mechanically stretched DNA. At higher stretching forces, ANKLE1 cleaves both strands of negatively supercoiled DNA, mirroring conditions in which stretched chromatin bridges lose histones to expose negatively supercoiled DNA. These findings show that ANKLE1 acts as a DNA tension sensor that resolves stretched chromatin bridges. Our study highlights the significance of mechanical forces in DNA bridge processing, enhances our understanding of how cells preserve genome integrity during cell division. - Source: PubMed
Publication date: 2025/12/08
Jiang HuadongHe FeiKong NannanLong JiePoon Yu ChingPunatar Rajvee ShahXu ZhichunZhai YuanliangWest Stephen CEfremov Artem KChan Ying Wai