ArticleThe Biochemical journal2005
The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 109 citations in OpenAlex.
- Impairment of novelty-dependent hippocampal behavioural tagging in Septin5-deficient mice.Molecular brain · 2026Article
- Septin5 deficiency impairs both recent and remote contextual fear memory.Molecular brain · 2025Article
- Septin5 deletion enhances β-cell exocytosis by releasing microtubule-tethered insulin granules onto plasma membrane.Nature communications · 2025Article
- Functional regulation of syntaxin-1: An underlying mechanism mediating exocytosis in neuroendocrine cells.Frontiers in endocrinology · 2023Review
- Septin-5 and -7-IgGs: Neurologic, Serologic, and Pathophysiologic Characteristics.Annals of neurology · 2022Article
- Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and localizes to autophagosomes during induced autophagy.Cellular and molecular life sciences : CMLS · 2022Article
- Right place, right time - Spatial guidance of neuronal morphogenesis by septin GTPases.Current opinion in neurobiology · 2022Review
- Biochemical and morphological characterization of SEPT1 in mouse brain.Medical molecular morphology · 2020Article
- The septin cytoskeleton regulates natural killer cell lytic granule release.The Journal of cell biology · 2020Article
- Production and analysis of a mammalian septin hetero-octamer complex.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Synaptic and Gene Regulatory Mechanisms in Schizophrenia, Autism, and 22q11.2 Copy Number Variant-Mediated Risk for Neuropsychiatric Disorders.Biological psychiatry · 2020Article
- In the line-up: deleted genes associated with DiGeorge/22q11.2 deletion syndrome: are they all suspects?Journal of neurodevelopmental disorders · 2019Review
- An Interaction Network of the Human SEPT9 Established by Quantitative Mass Spectrometry.G3 (Bethesda, Md.) · 2019Article
- A SEPT1-based scaffold is required for Golgi integrity and function.Journal of cell science · 2019Article
- Further reducingNeurology(R) neuroimmunology & neuroinflammation · 2018Article
- Critical reappraisal of mechanistic links of copy number variants to dimensional constructs of neuropsychiatric disorders in mouse models.Psychiatry and clinical neurosciences · 2018Review
- Glucose Transporters in Diabetic Kidney Disease-Friends or Foes?Frontiers in endocrinology · 2018Review
- Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens.Proteomes · 2017Article
- Uncovering the Roles of Septins in Cilia.Frontiers in cell and developmental biology · 2017Review
- Expression ofFrontiers in neuroanatomy · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins are supposed to mediate the docking and/or fusion of the vesicle with the plasma membrane. However, it is not clearly understood how this process is regulated. In a search for potential SNARE regulators, we recently identified septin 5 (Sept5) as a novel SNARE interacting protein. Septins were first identified as filamentous proteins required for cytokinesis in yeast. Several septins have now been identified in mammals but little is known about their functions. We have previously shown that Sept5 is predominantly expressed in the brain, where it associates with vesicles and membranes through its interaction with the SNARE domain of syntaxin 1A. Furthermore, Sept5 appears to inhibit exocytosis, possibly by regulating vesicle targeting and/or fusion events. To gain insight into the role of Sept5, we have mapped the Sept5 domains important for syntaxin binding. We also investigated the ability of Sept5 to bind to syntaxin when in various protein complexes. Although Sept5 cannot bind an nSec1-syntaxin complex, it can bind syntaxin in a SNARE complex. This interaction is occluded by the binding of alpha-SNAP, suggesting that Sept5 may regulate the availability of SNARE proteins through its interaction with syntaxin and the 7 S complex.
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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.