ArticleiScience2019
Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity.
Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- Reconstruction of septin higher-order nano-size structures in ovarian cancer cells uncover susceptibility to the septin-targeting small molecule UR214-9.bioRxiv : the preprint server for biology · 2026Article
- Non-decameric NLRP3 reveals a TGN/MTOC-distal pathway of inflammasome activation.Nature communications · 2026Article
- Study of Protein-Protein Interactions in Septin Assembly: Multiple amphipathic helix domains cooperate in binding to the lipid membrane.PLoS computational biology · 2026Article
- Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026Article
- Animal septins contain functional transmembrane domains.Current biology : CB · 2025Article
- Animal septins contain functional transmembrane domains.bioRxiv : the preprint server for biology · 2025Article
- Septin 9 expression regulates 'don't eat me' signals and identifies an immune-epithelial class of intrahepatic cholangiocarcinoma.Molecular oncology · 2024Article
- SEPT9_i1 and Septin Dynamics in Oncogenesis and Cancer Treatment.Biomolecules · 2024Review
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024Article
- Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024Article
- The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024Article
- Article
- Septins as membrane influencers: direct play or in association with other cytoskeleton partners.Frontiers in cell and developmental biology · 2023Review
- Septin 9 and phosphoinositides regulate lysosome localization and their association with lipid droplets.iScience · 2022Article
- Spatial regulation of microtubule-dependent transport by septin GTPases.Trends in cell biology · 2021Review
- PIAS1 Regulates Hepatitis C Virus-Induced Lipid Droplet Accumulation by Controlling Septin 9 and Microtubule Filament Assembly.Pathogens (Basel, Switzerland) · 2021Article
- Article
- A septin GTPase scaffold of dynein-dynactin motors triggers retrograde lysosome transport.The Journal of cell biology · 2021Article
- Septins From Protists to People.Frontiers in cell and developmental biology · 2021Review
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Septins are GTP-binding proteins involved in several membrane remodeling mechanisms. They associate with membranes, presumably using a polybasic domain (PB1) that interacts with phosphoinositides (PIs). Membrane-bound septins assemble into microscopic structures that regulate membrane shape. How septins interact with PIs and then assemble and shape membranes is poorly understood. Here, we found that septin 9 has a second polybasic domain (PB2) conserved in the human septin family. Similar to PB1, PB2 binds specifically to PIs, and both domains are critical for septin filament formation. However, septin 9 membrane association is not dependent on these PB domains, but on putative PB-adjacent amphipathic helices. The presence of PB domains guarantees protein enrichment in PI-contained membranes, which is critical for PI-enriched organelles. In particular, we found that septin 9 PB domains control the assembly and functionality of the Golgi apparatus. Our findings offer further insight into the role of septins in organelle morphology.
Indexed as
Identifiers
What OpenQuestion holds
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.