---
title: "FMNL1-mediated actin assembly completes mitochondrial division downstream of TGN vesicles"
id: "biorxiv-7-fmnl1-polymerized-actin-filaments-complete-mitochondrial-division-downstream-of"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-7-fmnl1-polymerized-actin-filaments-complete-mitochondrial-division-downstream-of"
content_type: "clinical_feed_article"
specialty: "General"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.10.21.760700v1?rss=1"
published_at: "2026-10-23T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# FMNL1-mediated actin assembly completes mitochondrial division downstream of TGN vesicles
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-7-fmnl1-polymerized-actin-filaments-complete-mitochondrial-division-downstream-of
- **Specialty:** [General](https://medichelpline.com/clinical-feed/general.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.10.21.760700v1?rss=1)
- **Published At:** 2026-10-23T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The study reported that **FMNL1**, a formin family actin assembly factor, is recruited to mitochondrial division sites via trans-Golgi network (TGN)–derived vesicles in a calcium-dependent pathway. - Investigators observed that **Cdc42** specifically activates **FMNL1**, which then nucleates **actin** filaments that complete outer mitochondrial membrane (**OMM**) scission in a **Drp1**- and actin-dependent process. - Depletion of **FMNL1** produced an accumulation of early division events: increased ER–mitochondrial contacts and higher recruitment of **Drp1** and TGN vesicles to mitochondria were documented, but final mitochondrial division failed. - The cohort of experiments indicates a downstream role for FMNL1 after vesicle delivery; in other words, TGN vesicle arrival and Drp1 recruitment occur but are not sufficient without FMNL1-driven filament assembly. - The authors declared no competing interests and acknowledged NIH National Institute of General Medical Sciences funding; methodological specifics such as live-cell imaging parameters, biochemical assays, exact depletion method, and quantitative endpoints were not reported in the source abstract. - Data indicated a calcium-dependence for FMNL1 recruitment; the source did not provide molecular details of the calcium sensor or the exact signaling intermediates linking TGN vesicles to FMNL1 activation. - The paper frames FMNL1 as a necessary executioner for OMM scission in the described pathway, while leaving open mechanistic questions about how FMNL1 activity is temporally coordinated with Drp1-mediated constriction.
## Clinical Analysis & Structured Key Points
FMNL1 polymerized actin filaments complete mitochondrial division downstream of Golgi-derived vesicles | bioRxiv Skip to main content New Results FMNL1 polymerized actin filaments complete mitochondrial division downstream of Golgi-derived vesicles Brandon Tabori , Amrapali Ghosh , Maite R Zavala , Rajarshi Chakrabarti doi: https://doi.org/10.64898/2026.10.21.760700 Brandon Tabori Thomas Jefferson University Find this author on Google Scholar Find this author on PubMed Search for this author on this site Amrapali Ghosh Thomas Jefferson University Find this author on Google Scholar Find this author on PubMed Search for this author on this site Maite R Zavala Thomas Jefferson University Find this author on Google Scholar Find this author on PubMed Search for this author on this site Rajarshi Chakrabarti Thomas Jefferson University Find this author on Google Scholar Find this author on PubMed Search for this author on this site For correspondence: rajarshi.chakrabarti{at}jefferson.edu Abstract Info/History Metrics Preview PDF Abstract Mitochondrial division includes contributions from several organelles yet the molecular machinery that facilitates the final Drp1-induced scission of the OMM is largely elusive. We elucidate that FMNL1, a formin family actin assembly factor, is recruited to the mitochondrial division sites through the TGN vesicles in a calcium dependent pathway to complete mitochondrial division. FMNL1 is activated specifically by Cdc42 that generates actin filaments to complete division of the OMM in Drp1 and actin-dependent pathway. Depletion of FMNL1 enhances early events in mitochondrial division pathway characterized by enhanced ER-mitochondrial contacts and increased Drp1 and TGN vesicles on mitochondria which still results in failed mitochondrial division. Competing Interest Statement The authors have declared no competing interest. Funder Information Declared National Institute of General Medical Sciences, https://ror.org/04q48ey07 , NIH R35 GM150811-3 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-NC 4.0 International license . Back to top Previous Next Posted October 23, 2026. Download PDF Email Thank you for your interest in spreading the word about bioRxiv. NOTE: Your email address is requested solely to identify you as the sender of this article. Your Email * Your Name * Send To * Enter multiple addresses on separate lines or separate them with commas. You are going to email the following FMNL1 polymerized actin filaments complete mitochondrial division downstream of Golgi-derived vesicles Message Subject (Your Name) has forwarded a page to you from bioRxiv Message Body (Your Name) thought you would like to see this page from the bioRxiv website. Your Personal Message CAPTCHA This question is for testing whether or not you are a human visitor and to prevent automated spam submissions. Share FMNL1 polymerized actin filaments complete mitochondrial division downstream of Golgi-derived vesicles Brandon Tabori , Amrapali Ghosh , Maite R Zavala , Rajarshi Chakrabarti bioRxiv 2026.10.21.760700; doi: https://doi.org/10.64898/2026.10.21.760700 Share This Article: Copy Citation Tools FMNL1 polymerized actin filaments complete mitochondrial division downstream of Golgi-derived vesicles Brandon Tabori , Amrapali Ghosh , Maite R Zavala , Rajarshi Chakrabarti bioRxiv 2026.10.21.760700; doi: https://doi.org/10.64898/2026.10.21.760700 Citation Manager Formats BibTeX Bookends EasyBib EndNote (tagged) EndNote 8 (xml) Medlars Mendeley Papers RefWorks Tagged Ref Manager RIS Zotero Tweet Widget Facebook Like Google Plus One Subject Areas All Articles Animal Behavior and Cognition (8164) Biochemistry (19027) Bioengineering (15171) Bioinformatics (45323) Biophysics (22958) Cancer Biology (20106) Cell Biology (27293) Clinical Trials (138) Developmental Biology (14142) Ecology (21393) Epidemiology (2067) Evolutionary Biology (25782) Genetics (16342) Genomics (23827) Immunology (19017) Microbiology (43178) Molecular Biology (18335) Neuroscience (95039) Paleontology (712) Pathology (3031) Pharmacology and Toxicology (5197) Physiology (8278) Plant Biology (16266) Scientific Communication and Education (2115) Synthetic Biology (4643) Systems Biology (10382) Zoology (2426)
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