ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2022
A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2022. 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, 19 citations in OpenAlex.
- Myosin IIA motor regulates attaching-effacing bacteria interactions with intestinal epithelium.Gut microbes · 2026Article
- Primary human intestinal organoids with biallelic UNC45A variants suggest role of cystic fibrosis transmembrane conductance regulator in pathogenesis of UNC45A-related intestinal disorder.Journal of pediatric gastroenterology and nutrition · 2026Article
- The septin cytoskeleton is a regulator of intestinal epithelial barrier integrity and mucosal inflammation.JCI insight · 2025Article
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome.JCI insight · 2025Article
- Intestinal Epithelial Tight Junction Barrier Regulation by Novel Pathways.Inflammatory bowel diseases · 2025Review
- Multi-omics integration analysis based on plasma circulating proteins reveals potential therapeutic targets for ulcerative colitis.Frontiers in molecular biosciences · 2025Article
- Review
- Coactosin-like protein 1 regulates integrity and repair of model intestinal epithelial barriers via actin binding dependent and independent mechanisms.Frontiers in cell and developmental biology · 2024Article
- Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.The Journal of cell biology · 2023Article
- Complexification of In Vitro Models of Intestinal Barriers, A True Challenge for a More Accurate Alternative Approach.International journal of molecular sciences · 2023Review
- Understanding disruption of the gut barrier during inflammation: Should we abandon traditional epithelial cell lines and switch to intestinal organoids?Frontiers in immunology · 2023Review
- A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Case report: Osteo-oto-hepato-enteric syndrome caused by UNC45A deficiency.Frontiers in genetics · 2022Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
The actomyosin cytoskeleton serves as a key regulator of the integrity and remodeling of epithelial barriers by controlling assembly and functions of intercellular junctions and cell-matrix adhesions. Although biochemical mechanisms that regulate the activity of non-muscle myosin II (NM-II) in epithelial cells have been extensively investigated, little is known about assembly of the contractile myosin structures at the epithelial adhesion sites. UNC-45A is a cytoskeletal chaperone that is essential for proper folding of NM-II heavy chains and myofilament assembly. We found abundant expression of UNC-45A in human intestinal epithelial cell (IEC) lines and in the epithelial layer of the normal human colon. Interestingly, protein level of UNC-45A was decreased in colonic epithelium of patients with ulcerative colitis. CRISPR/Cas9-mediated knock-out of UNC-45A in HT-29cf8 and SK-CO15 IEC disrupted epithelial barrier integrity, impaired assembly of epithelial adherence and tight junctions and attenuated cell migration. Consistently, decreased UNC-45 expression increased permeability of the Drosophila gut in vivo. The mechanisms underlying barrier disruptive and anti-migratory effects of UNC-45A depletion involved disorganization of the actomyosin bundles at epithelial junctions and the migrating cell edge. Loss of UNC-45A also decreased contractile forces at apical junctions and matrix adhesions. Expression of deletion mutants revealed roles for the myosin binding domain of UNC-45A in controlling IEC junctions and motility. Our findings uncover a novel mechanism that regulates integrity and restitution of the intestinal epithelial barrier, which may be impaired during mucosal inflammation.
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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.