ArticleJournal of molecular biology2015
Septin 9 Exhibits Polymorphic Binding to F-Actin and Inhibits Myosin and Cofilin Activity.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
55 citing papers in PubMed, 94 citations in OpenAlex.
- Evolutionarily conserved short linear motifs drive actin filament binding.Nature cell biology · 2026Article
- Microtubule-templated actin assembly by septin9 drives apical expansion of epithelial cells.bioRxiv : the preprint server for biology · 2026Article
- Septin crosstalk with microtubules and actin is regulated by a GSK3-dependent phosphoswitch.bioRxiv : the preprint server for biology · 2026Article
- Local RhoA activation induces anillin-independent septin recruitment in interphase cells.Molecular biology of the cell · 2026Article
- Septins buffer actomyosin forces to protect the nucleus from genotoxic mechanical stress.bioRxiv : the preprint server for biology · 2026Article
- The septin cytoskeleton is a regulator of intestinal epithelial barrier integrity and mucosal inflammation.JCI insight · 2025Article
- SEPT9 methylation as a diagnostic and predictive biomarker in the progression of ductal carcinoma in situ to invasive breast cancer.Scientific reports · 2025Article
- Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025Article
- Dysregulation of septin cytoskeletal organization in the trabecular meshwork contributes to ocular hypertension.JCI insight · 2024Article
- Borg5 restricts contractility and motility in epithelial MDCK cells.Journal of cell science · 2024Article
- Genome-Wide Association Study and Phenotype Prediction of Reproductive Traits in Large White Pigs.Animals : an open access journal from MDPI · 2024Article
- SEPT9_i1 and Septin Dynamics in Oncogenesis and Cancer Treatment.Biomolecules · 2024Review
- Article
- An oncogenic isoform of septin 9 promotes the formation of juxtanuclear invadopodia by reducing nuclear deformability.Cell reports · 2023Article
- A census of actin-associated proteins in humans.Frontiers in cell and developmental biology · 2023Article
- Coordinated regulation of Cdc42ep1, actin, and septin filaments during neural crest cell migration.Frontiers in cell and developmental biology · 2023Article
- Septins as membrane influencers: direct play or in association with other cytoskeleton partners.Frontiers in cell and developmental biology · 2023Review
- Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Localization Patterns of RAB3C Are Associated with Murine and Human Sperm Formation.Medicina (Kaunas, Lithuania) · 2022Article
- Septin 9 and phosphoinositides regulate lysosome localization and their association with lipid droplets.iScience · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Septins are a highly conserved family of proteins in eukaryotes that is recognized as a novel component of the cytoskeleton. Septin 9 (SEPT9) interacts directly with actin filaments and functions as an actin stress fiber cross-linking protein that promotes the maturation of nascent focal adhesions and cell migration. However, the molecular details of how SEPT9 interacts with F-actin remain unknown. Here, we use electron microscopy and image analysis to show that SEPT9 binds to F-actin in a highly polymorphic fashion. We demonstrate that the basic domain (B-domain) of the N-terminal tail of SEPT9 is responsible for actin cross-linking, while the GTP-binding domain (G-domain) does not bundle F-actin. We show that the B-domain of SEPT9 binds to three sites on F-actin, and the two of these sites overlap with the binding regions of myosin and cofilin. SEPT9 inhibits actin-dependent ATPase activity of myosin and competes with the weakly bound state of myosin for binding to F-actin. At the same time, SEPT9 significantly reduces the extent of F-actin depolymerization by cofilin. Taken together, these data suggest that SEPT9 protects actin filaments from depolymerization by cofilin and myosin and indicate a mechanism by which SEPT9 could maintain the integrity of growing and contracting actin filaments.
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Registered trials
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.