{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"medRxiv"}],"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T16:48:36Z","timestamp":1774716516338,"version":"3.50.1"},"posted":{"date-parts":[[2026,3,26]]},"group-title":"Nephrology","reference-count":77,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T00:00:00Z","timestamp":1774483200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.medrxiv.org\/about\/FAQ#license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,3,26]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                <jats:p>\n                  Poor outcomes in proteinuric kidney diseases are challenging to successfully manage therapeutically due to the heterogeneity of underlying disease pathogenesis and associated risk for progression. The role of cytoskeleton-associated proteins, including the scaffolding protein Anillin (ANLN), are of specific interest in kidney disease given the importance of actin dynamics in the kidney\u2019s specialized epithelial cell types. In this study, we identify the prevalence of genetic variants in\n                  <jats:italic>ANLN<\/jats:italic>\n                  , the gene encoding ANLN, in a cohort of deeply phenotyped individuals with non-diabetic proteinuric kidney disease. Thirty-one individuals (of 864 genotyped) harbor heterozygously expressed variants in\n                  <jats:italic>ANLN<\/jats:italic>\n                  ; 7 unrelated individuals shared the same variant (I1109V) in the C-terminal pleckstrin homology (PH) domain, a region necessary for interaction with the plasma membrane. Kidney organoids generated from I1109V induced pluripotent stem cells from 1 of these individuals showed increased epithelial cell mitogen-activated protein kinase 8 network activity and apoptosis, which was enhanced by tumor necrosis factor alpha (TNF-\u03b1) and phenocopied by actin polymerization inhibition. TNF-\u03b1-treated I1109V organoids also exhibited tubular lumen expansion. Knockdown and re-expression of the analogous ANLN variant in\n                  <jats:italic>Xenopus laevis<\/jats:italic>\n                  embryonic epithelia resulted in defects in cell-cell junction dynamics including wavy cell membranes exhibiting increased transverse movements as well as abnormal junctional F-actin remodeling in response to mechanical stress and leaky barrier function. Taken together, these results indicate that enhanced tubular epithelial cell death, perturbed cell-cell contacts and barrier function defects are associated with a novel ANLN variant discovered in individuals with non-diabetic proteinuric kidney disease.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>ONE SENTENCE SUMMARY<\/jats:title>\n                  <jats:p>Enhanced tubular epithelial cell death and perturbed cell-cell junction integrity and barrier function are associated with a novel Anillin coding variant discovered in a cohort of individuals with proteinuric kidney disease.<\/jats:p>\n                <\/jats:sec>","DOI":"10.64898\/2026.03.24.26348901","type":"posted-content","created":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T18:30:25Z","timestamp":1774549825000},"source":"Crossref","is-referenced-by-count":0,"title":["Anillin variant in proteinuric kidney disease drives tubular epithelial cell death, junctional instability, and barrier dysfunction"],"prefix":"10.64898","author":[{"given":"Zie","family":"Craig","sequence":"first","affiliation":[{"name":"Department of Molecular, Cellular, and Developmental Biology, University of Michigan; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3250-8258","authenticated-orcid":false,"given":"Holly M.","family":"Jacobs","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Damian","family":"Fermin","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew","family":"Fischer","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoyun","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of Mechanical Engineering, Whiting School of Engineering, Johns Hopkins University; Baltimore, MD 21218, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Celine C.","family":"Berthier","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jalen A.","family":"Smith","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular, and Developmental Biology, University of Michigan; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jamal","family":"El Saghir","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; Ann Arbor, MI 48109, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sean","family":"Eddy","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, Division of Nephrology, University of Michigan Medical School; 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