---
title: "MYO1E missense variants A92E and G562R impair Myo1e localization and motor activity in steroid-res"
id: "biorxiv-18-disease-associated-amino-acid-substitutions-outside-canonical-motor-motifs"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-18-disease-associated-amino-acid-substitutions-outside-canonical-motor-motifs"
content_type: "clinical_feed_article"
specialty: "Nephrology"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1?rss=1"
published_at: "2026-10-19T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# MYO1E missense variants A92E and G562R impair Myo1e localization and motor activity in steroid-res
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-18-disease-associated-amino-acid-substitutions-outside-canonical-motor-motifs
- **Specialty:** [Nephrology](https://medichelpline.com/clinical-feed/nephrology.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1?rss=1)
- **Published At:** 2026-10-19T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The preprint reports two **MYO1E** missense variants, A92E and G562R, found in trans in a patient with childhood-onset **steroid-resistant nephrotic syndrome (SRNS)**. - Both substitutions lie outside canonical P-loop and switch subdomains of the Myo1e motor domain yet affect highly conserved residues predicted to reside in α-helices. - Structural prediction suggested replacement by larger, charged residues that may destabilize folding or reduce protein stability. - In cultured podocyte-derived cells, both mutants failed to localize to intercellular junctions and showed reduced colocalization with the actin cytoskeleton. - The G562R variant formed cytoplasmic aggregates in a manner partially dependent on expression level; this variant also had decreased fluorescence recovery after photobleaching, indicating altered protein dynamics. - Biochemical assays revealed markedly reduced ATPase activity for G562R; A92E retained ATPase activity similar to wild-type but displayed reduced in vitro motility and decreased thermal stability. - The authors conclude that A92E and G562R compromise **Myo1e** localization and function and argue these effects support pathogenicity in SRNS. - The article is a preprint and has not been certified by peer review; the source did not report additional clinical or population-level data beyond the single patient, nor did it report in vivo phenotypes or rescue experiments in animal models.
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Kazi Sayeeda 1 SUNY Upstate Medical University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Kazi%2BSayeeda%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Sayeeda%20K&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AKazi%2BSayeeda%2B) * [ORCID record for Kazi Sayeeda](http://orcid.org/0009-0008-5433-1311 "Open in new tab") Jinghua Ge 2 Penn State College of Medicine * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Jinghua%2BGe%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Ge%20J&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AJinghua%2BGe%2B) * [ORCID record for Jinghua Ge](http://orcid.org/0000-0002-5820-1521 "Open in new tab") Christopher M Yengo 2 Penn State College of Medicine * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Christopher%2BM%2BYengo%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Yengo%20CM&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AChristopher%2BM%2BYengo%2B) * [ORCID record for Christopher M Yengo](http://orcid.org/0000-0003-3987-9019 "Open in new tab") Mira Krendel 1 SUNY Upstate Medical University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Mira%2BKrendel%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Krendel%20M&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AMira%2BKrendel%2B) * [ORCID record for Mira Krendel](http://orcid.org/0000-0002-7008-9069 "Open in new tab") * For correspondence: krendelm@upstate.edu * [Abstract](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5882350/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5882350/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5882350/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5882350/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5882350/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract Steroid-resistant nephrotic syndrome (SRNS) is a severe kidney disorder characterized by proteinuria and disruption of glomerular filtration, often driven by genetic defects in genes encoding proteins required for podocyte functions. Among these, MYO1E, encoding the actin- and membrane-associated motor protein Myosin 1e (Myo1e), has been implicated in familial and sporadic forms of SRNS. Here, we investigated two MYO1E missense variants, A92E and G562R, identified in trans in a patient with childhood-onset SRNS and located outside canonical P-loop and switch subdomains of the Myo1e motor domain. Both residues are highly conserved, located within predicted α-helices in the motor domain, and replaced by larger charged residues, which may reduce protein stability or folding. In podocyte-derived cells, both mutants failed to localize at intercellular junctions and displayed reduced colocalization with actin. The G562R variant additionally formed cytoplasmic aggregates that were partially expression-level-dependent and exhibited decreased fluorescence recovery after photobleaching, indicating impaired protein dynamics. In vitro motility and ATPase assays indicated that the G562R mutant exhibited a marked loss of ATPase activity while the A92E mutant displayed ATPase activity similar to the WT but was characterized by reduced motility and thermal stability. Together, these results demonstrate that A92E and G562R mutations compromise Myo1e localization and function, supporting their pathogenic role in SRNS. ### Competing Interest Statement The authors have declared no competing interest. ## Funder Information Declared National Institute of Diabetes and Digestive and Kidney Diseases, R01DK083345 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY 4.0 International license](http://creativecommons.org/licenses/by/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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[ Download PDF](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.full.pdf) Print/Save Options [Download PDF](https://www.biorxiv.org/content/biorxiv/early/2026/10/19/2026.10.15.759198.full.pdf)Full Text & In-line FiguresXML [More Info](https://www.biorxiv.org/about/FAQ#PrintOptions "More Information on Print/Save Options") [Supplementary Material ](https://www.biorxiv.org/content/10.64898/2026.10.15.759198v1.supplementary-material) [ Email](https://www.biorxiv.org/ "Email this Article") [ Share](https://www.biorxiv.org/) Disease-associated amino acid substitutions outside canonical motor motifs impair Myo1e localization and activity Kazi Sayeeda, Jinghua Ge, Christopher M Yengo, Mira Krendel bioRxiv 2026.10.15.759198; doi: https://doi.org/10.64898/2026.10.15.759198 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. 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