ArticleCytoskeleton (Hoboken, N.J.)2019
Regulation of microtubule plus end dynamics by septin 9.
Article in Cytoskeleton (Hoboken, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- 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
- A structured framework of cytoskeletal proteins and noncentrosomal microtubules promotes the initiation and elongation of invadopodia.Molecular biology of the cell · 2025Article
- Extensive methylation analysis of circulating tumor DNA in plasma of patients with gastric cancer.Scientific reports · 2024Article
- SEPT9_i1 and Septin Dynamics in Oncogenesis and Cancer Treatment.Biomolecules · 2024Review
- MiR-503-5p alleviates peripheral neuropathy-induced neuropathic pain in T2DM mice by regulating SEPT9 to inhibit astrocyte activation.Scientific reports · 2024Article
- Reconstitution of Neuronal Motor Traffic on Septin-Associated Microtubules.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Nanoscale details of mitochondrial constriction revealed by cryoelectron tomography.Biophysical journal · 2023Article
- 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
- Right place, right time - Spatial guidance of neuronal morphogenesis by septin GTPases.Current opinion in neurobiology · 2022Review
- Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers.International journal of molecular sciences · 2022Article
- SNHG3 Affects Gastric Cancer Development by Regulating SEPT9 Methylation.Journal of oncology · 2022Article
- Spatial regulation of microtubule-dependent transport by septin GTPases.Trends in cell biology · 2021Review
- Article
- Cellular functions of actin- and microtubule-associated septins.Current biology : CB · 2021Review
- The state of the septin cytoskeleton from assembly to function.Current opinion in cell biology · 2021Review
- The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021Review
- Production and analysis of a mammalian septin hetero-octamer complex.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020Review
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Septins are GTP-binding proteins that associate with the microtubule (MT) and actin cytoskeleton. Septins affect MT organization and posttranslational modifications, but their role in MT dynamics is less understood. Here, we reconstituted MT dynamics in the presence of the MT-binding septin (SEPT9) using an in vitro cell-free assay, which images the polymerization of tubulin from guanosine-5'-[(α,β)-methyleno]triphosphate (GMPCPP)-stabilized MT seeds. We found that submicromolar concentrations of SEPT9 suppress MT catastrophe and enhance the growth of MT plus ends to great lengths, while low micromolar concentrations of SEPT9 stabilize MTs by inhibiting dynamic instability. We show that SEPT9 associates preferentially with the lattice of GMPCPP-stabilized MT seeds and surprisingly recruits soluble tubulin to the MT lattice. Notably, the effects of SEPT9 on MT dynamics are dependent on its G-G dimerization interface, which is formed by the pockets of the GTP-binding domains. A mutation (H530D) that disrupts G-G dimerization abrogates the effects of SEPT9 on MT dynamics and diminishes its ability to recruit tubulin to the MT lattice. Taken together, these results suggest that SEPT9 promotes the formation and maintenance of long stable MTs through a mechanism that may involve recruitment of unpolymerized tubulin to the MT lattice.
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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.