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Showing SEPTIN5 — SEPT5 is a alias.

SEPTIN5

Septin-5 · UniProt Q99719

Length
369 aa
Mass
42.8 kDa
Annotated
2026-06-10
42 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SEPTIN5 (CDCrel-1/SEPT5) is a presynaptic GTPase of the septin family that acts as a brake on regulated exocytosis by physically gating the SNARE machinery (PMID:10321247, PMID:9760144). It binds syntaxin-1A directly through a defined SNARE interaction domain, and the GTPase activity is required for its inhibitory effect: wild-type SEPTIN5 suppresses secretion whereas dominant-negative GTPase mutants enhance it (PMID:10321247). Mechanistically, SEPTIN5 engages syntaxin within the assembled 7S SNARE complex but is excluded by alpha-SNAP, with which it competes for access, thereby regulating SNARE availability (PMID:15355307). This inhibitory binding is switched off by Cdk5/p35-mediated phosphorylation at Ser17 and Ser327, which lowers syntaxin affinity; non-phosphorylatable mutants bind syntaxin more tightly and potentiate exocytosis, linking the modification to secretion and to short-term synaptic plasticity (PMID:17224448, PMID:18385322, PMID:34954322). Beyond the SNARE interface, SEPTIN5 assembles into heteromeric septin filaments with Nedd5, CDC10, Sept3, Sept7, and Sept11 and localizes to microtubule–plasma membrane contact sites, where in pancreatic beta-cells it anchors secretory granules away from the plasma membrane; its deletion destabilizes the cortical microtubule meshwork and markedly enhances glucose-stimulated insulin secretion (PMID:11739749, PMID:17564677, PMID:40108136). SEPTIN5 is a substrate of the E3 ubiquitin ligase parkin (with E2 UbcH8), which ubiquitinates it for proteasomal degradation; familial Parkinson's disease parkin mutations impair this turnover, and SEPTIN5 accumulation drives dopamine-dependent dopaminergic neurodegeneration (PMID:11078524, PMID:14559152, PMID:14530399). Downregulation of SEPTIN5 additionally promotes autophagosomal degradation of APP C-terminal fragments and lowers Aβ, connecting it to amyloid processing (PMID:33203136).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1998 Medium

    Establishing where SEPTIN5 acts was the first step: localizing the protein to presynaptic terminals framed it as a candidate regulator of neurotransmission.

    Evidence Immunohistochemistry and synaptosomal co-purification with SNAP-25 and synaptophysin in human brain

    PMID:9760144

    Open questions at the time
    • Did not define a molecular partner or function
    • Subcellular resolution limited to fractionation
  2. 1999 High

    This defined SEPTIN5's core function — it binds syntaxin-1A and inhibits exocytosis in a GTPase-dependent manner, identifying it as a SNARE-targeting brake on secretion.

    Evidence Co-IP, direct binding, and wild-type vs dominant-negative GTPase mutant secretion assays in HIT-T15 cells

    PMID:10321247

    Open questions at the time
    • Did not resolve whether binding is to free or assembled syntaxin
    • GTP cycle regulation of the interaction unmapped
  3. 2000 High

    Identifying parkin as the E3 ligase for SEPTIN5 connected its turnover to the proteasome and to Parkinson's disease genetics.

    Evidence In vitro ubiquitination with UbcH8, Co-IP, cell-based degradation assay, and parkin RING-domain mutagenesis

    PMID:11078524

    Open questions at the time
    • Did not show SEPTIN5 accumulation drives neuronal death
    • Ubiquitination site on SEPTIN5 not mapped
  4. 2002 High

    Genetic knockout and complex analysis tested whether SEPTIN5 is essential and revealed it operates within redundant heteromeric septin filaments.

    Evidence Co-IP of Nedd5/CDC10 complexes, KIAA0202 yeast two-hybrid/pull-down, and CDCrel-1 knockout mouse phenotyping

    PMID:11739749 PMID:12023038

    Open questions at the time
    • Knockout had no overt synaptic phenotype, leaving in vivo function ambiguous
    • Compensation by other septins not directly proven
  5. 2003 High

    Linking parkin-dependent SEPTIN5 turnover to disease showed that SEPTIN5 accumulates in patient brain and is neurotoxic when overexpressed, establishing causal relevance to dopaminergic degeneration.

    Evidence Co-IP from human substantia nigra, in vitro ubiquitination of splice variants, post-mortem brain analysis, and AAV overexpression in rat substantia nigra with dopamine-dependent rescue

    PMID:14530399 PMID:14559152

    Open questions at the time
    • Mechanism linking accumulation to dopamine toxicity not fully defined
    • Endogenous SEPTIN5 levels in sporadic PD not addressed
  6. 2005 High

    Defining the binding interface mechanistically showed SEPTIN5 targets the assembled 7S SNARE complex and competes with alpha-SNAP, explaining how it gates SNARE recycling/availability.

    Evidence In vitro domain mapping and competitive binding assays with purified SNARE complexes and alpha-SNAP

    PMID:15355307

    Open questions at the time
    • Stoichiometry of competition in vivo unknown
    • Effect on SNARE disassembly kinetics not measured
  7. 2007 High

    Discovery of Cdk5/p35 phosphorylation at Ser17 provided the regulatory switch that detaches SEPTIN5 from syntaxin, coupling the brake to a kinase signal.

    Evidence MS substrate identification, in vitro kinase assay, Ser17 mutagenesis, GST pull-down and synaptosomal Co-IP

    PMID:17224448

    Open questions at the time
    • Functional secretion consequence of Ser17 not directly assayed here
    • Isoform specificity of the site
  8. 2007 Medium

    Mapping further septin partners (Sept3, Sept7) at nerve terminals reinforced that SEPTIN5 functions as part of synaptic septin filaments near vesicle pools.

    Evidence Direct binding assays and co-localization with synaptophysin in hippocampal neurons; Sept3 knockout

    PMID:17564677

    Open questions at the time
    • Filament architecture not resolved
    • Functional output of the Sept3/5/7 complex untested
  9. 2008 High

    A second Cdk5 site (Ser327) was shown to functionally tune exocytosis, with a phospho-dead mutant binding syntaxin better and potentiating secretion — directly tying phosphorylation to release.

    Evidence Kinase assays, S327A mutagenesis, Co-IP from Cdk5 KO vs WT lysates, PC12 exocytosis assay

    PMID:18385322

    Open questions at the time
    • Relative contribution of Ser17 vs Ser327 in vivo unresolved
    • Upstream signals activating Cdk5 toward SEPTIN5 unknown
  10. 2010 Medium

    Identifying ARMS/Kidins220 as an N-terminal partner extended SEPTIN5's interactome to neurite-tip and plasma-membrane signaling scaffolds.

    Evidence Yeast two-hybrid, Co-IP from HEK-293, domain mapping, co-localization in neurons and PC12 cells

    PMID:20680483

    Open questions at the time
    • Functional consequence of the interaction undefined
    • Single-lab Co-IP without reciprocal endogenous validation
  11. 2020 High

    A new functional axis emerged: SEPTIN5 loss promotes autophagosomal clearance of APP C-terminal fragments and lowers Aβ, implicating it in amyloid metabolism independent of trafficking.

    Evidence shRNA knockdown and Septin5 KO mouse cortex, APP CTF/Aβ measurement, autophagy marker analysis, trafficking assays

    PMID:33203136

    Open questions at the time
    • Direct molecular link between SEPTIN5 and autophagy machinery not identified
    • Whether effect requires syntaxin/SNARE function unknown
  12. 2021 Medium

    Phosphomutant analysis tied the Ser327 modification to both APP processing/autophagy and to short-term synaptic plasticity, integrating SEPTIN5's secretory and amyloid roles under one regulatory mark.

    Evidence Lentiviral S327A/S327D in cortical neurons, APP and autophagy readouts, ex vivo CA3-CA1 electrophysiology

    PMID:34954322

    Open questions at the time
    • Causal chain from phosphorylation to autophagy unresolved
    • Single-lab functional correlations
  13. 2024 Medium

    New interactions with VMAT2 and palmitoylated Sept8 connected SEPTIN5 to monoamine handling and to vesicle-like structure formation, broadening its secretory-organelle associations.

    Evidence Co-IP from rat striatum with METH model; co-expression imaging with Sept8-204 palmitoylation manipulation (ZDHHC17/PPT1)

    PMID:38308620 PMID:39684782

    Open questions at the time
    • VMAT2 interaction shown by single Co-IP without reconstitution
    • Functional significance of Sept8/SEPT5 vesicle structures untested
  14. 2025 High

    Super-resolution and KO work in beta-cells unified the localization and secretory-brake themes: SEPTIN5 sits at microtubule–plasma membrane contact sites anchoring granules, and its loss destabilizes cortical microtubules to dramatically enhance insulin secretion.

    Evidence Super-resolution imaging, Septin5 KO rodent model, live granule dynamics, Ca2+ channel co-localization, insulin secretion in rodent and human islets

    PMID:40108136

    Open questions at the time
    • How GTP state controls contact-site assembly unknown
    • Link between microtubule role and SNARE-binding role not mechanistically bridged

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how SEPTIN5's two mechanistic faces — direct SNARE/syntaxin gating and cortical microtubule/granule anchoring — are coordinated, and how its GTPase cycle and phosphorylation jointly switch between them.
  • No structure of SEPTIN5 bound to the SNARE complex
  • GTP-cycle regulation of filament assembly vs syntaxin binding undefined
  • Direct effector linking SEPTIN5 to autophagy unidentified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 2 GO:0003924 GTPase activity 1
Localization
GO:0005886 plasma membrane 3 GO:0031410 cytoplasmic vesicle 2 GO:0005856 cytoskeleton 1
Pathway
R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-112316 Neuronal System 2 R-HSA-9612973 Autophagy 1
Partners
KIDINS220NEDD5PARK2SEPT11SEPT3SEPT7SLC18A2STX1A
Complex memberships
SNARE/7S complex (interacting)septin heteromeric complex (Sept3/Sept5/Sept7)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 SEPTIN5 (CDCrel-1) directly binds syntaxin-1A via the SNARE interaction domain, associates with synaptic vesicle membrane fractions, and co-immunoprecipitates with syntaxin and Nedd5. Overexpression of wild-type CDCrel-1 inhibited secretion in HIT-T15 cells, whereas GTPase dominant-negative mutants enhanced secretion, establishing SEPTIN5 as an inhibitor of exocytosis acting through syntaxin. Subcellular fractionation, co-immunoprecipitation, direct binding assay, transfection with wild-type and dominant-negative GTPase mutants in HIT-T15 cells Nature neuroscience High 10321247
2000 Parkin acts as an E3 ubiquitin-protein ligase (through its C-terminal RING-finger domains, with E2 enzyme UbcH8) that ubiquitinates and promotes proteasomal degradation of SEPTIN5 (CDCrel-1). Parkin binds SEPTIN5 through its RING-finger domains. Familial Parkinson's disease-linked parkin mutations disrupt this ubiquitin ligase function and impair SEPTIN5 degradation. In vitro ubiquitination assay, co-immunoprecipitation, cell-based degradation assay, site-directed mutagenesis of Parkin RING domains Proceedings of the National Academy of Sciences of the United States of America High 11078524
2002 SEPTIN5 (CDCrel-1) forms a heteromeric complex with septins Nedd5 and CDC10 in neurons. CDCrel-1 null mice show altered expression of other septins, suggesting functional redundancy within the septin complex. CDCrel-1 expression rises at synaptic maturation. Homozygous CDCrel-1 knockout mice display normal synaptic properties and hippocampal neuron growth in vitro. Co-immunoprecipitation, generation of CDCrel-1 knockout mice, electrophysiological and morphological analysis Molecular and cellular biology High 11739749
2002 SEPTIN5 (CDCrel-1) physically interacts with KIAA0202 (another human septin), as demonstrated by yeast two-hybrid and confirmed by GST pull-down and co-immunoprecipitation from the K-562 human leukemia cell line. Yeast two-hybrid, GST pull-down, co-immunoprecipitation FEBS letters Medium 12023038
2003 SEPT5_v2, a splice variant of SEPTIN5, is a parkin-binding protein. It binds parkin at the amino terminus and ring finger domains. Parkin ubiquitinates SEPT5_v2 in vitro, and both SEPT5_v1 and SEPT5_v2 accumulate in brains of autosomal-recessive juvenile parkinsonism patients, indicating parkin is essential for their normal turnover. Yeast two-hybrid screen, co-immunoprecipitation from human substantia nigra lysates, in vitro ubiquitination assay, post-mortem brain protein analysis Brain research. Molecular brain research High 14559152
2003 Overexpression of SEPTIN5 (CDCrel-1) in the substantia nigra via AAV-mediated gene transfer causes progressive loss of dopaminergic neurons in a dopamine-dependent manner. SEPTIN5 inhibits dopamine release from PC12 cells, and pharmacological inhibition of dopamine synthesis prevents CDCrel-1-induced neurodegeneration in vivo. AAV-mediated in vivo gene transfer to rat substantia nigra, dopaminergic neuron counting, striatal dopamine measurement, PC12 cell dopamine release assay, pharmacological inhibition Proceedings of the National Academy of Sciences of the United States of America High 14530399
2005 SEPTIN5 (Sept5) binds syntaxin within the assembled SNARE complex (7S complex), but cannot bind an nSec1-syntaxin complex. Alpha-SNAP binding to the SNARE complex occludes Sept5 binding, indicating Sept5 and alpha-SNAP compete for binding to the syntaxin-containing 7S complex, suggesting a regulatory role for Sept5 in SNARE availability. In vitro binding assays mapping Sept5 domains required for syntaxin binding, competitive binding assays with purified SNARE complexes and alpha-SNAP The Biochemical journal High 15355307
2006 SEPTIN5 (SEPT5) interacts with SEPT11 in human endothelial cells. The interaction requires the GTP-binding domain and C-terminal extension of SEPT11, confirmed by yeast two-hybrid, co-precipitation from JURKAT cell lysates, and FRET. Both proteins are co-expressed in HUVECs. Yeast two-hybrid, co-immunoprecipitation, FRET, domain deletion analysis The Journal of pathology Medium 16767699
2007 Cyclin-dependent kinase 5 (Cdk5)/p35 phosphorylates SEPTIN5 (Sept5_v1) at Ser17 in vitro and in mouse brain. Phosphorylation at Ser17 decreases binding of Sept5_v1 to syntaxin-1, as shown by co-immunoprecipitation from synaptosomal fractions and GST-syntaxin-1A pull-down assays. Mass spectrometry identification of Cdk5 substrates, in vitro kinase assay, site-directed mutagenesis (Ser17), GST pull-down, co-immunoprecipitation from synaptosomal fractions The Journal of biological chemistry High 17224448
2007 Sept3 directly binds Sept5 and Sept7 and forms a heteromeric complex at nerve terminals in mature neurons, adjacent to synaptophysin-positive synaptic vesicle regions, as demonstrated by direct binding assays and co-localization in hippocampal neurons. Direct binding assay, co-localization by immunofluorescence in primary neurons, Sept3 knockout mouse generation Journal of neurochemistry Medium 17564677
2008 Cdk5/p35 phosphorylates human SEPTIN5 (hCDCrel-1) at Ser327. Phosphorylation at S327 decreases SEPTIN5 binding to syntaxin-1 (shown by Co-IP from synaptic vesicle fractions and Cdk5 knockout lysates). A non-phosphorylatable S327A mutant binds syntaxin more efficiently than wild-type and potentiates regulated exocytosis more than wild-type when expressed in PC12 cells. Yeast two-hybrid screen, GST pull-down, co-immunoprecipitation, in vitro and in vivo phosphorylation assay, site-directed mutagenesis (S327A), PC12 cell exocytosis assay The Journal of neuroscience High 18385322
2010 ARMS/Kidins220 interacts with SEPTIN5 (Sept5) through the N-terminal region of Sept5. The interaction was confirmed by co-immunoprecipitation from HEK-293 cells. Endogenous proteins co-localize at the plasma membrane and neurite tips in hippocampal neurons and NGF-treated PC12 cells. Yeast two-hybrid, co-immunoprecipitation from transfected HEK-293 cells, domain mapping, co-localization in primary neurons and PC12 cells Molecules and cells Medium 20680483
2020 Downregulation of SEPTIN5 reduces levels of APP C-terminal fragments (APP CTFs) and Aβ in neuronal cells and in Septin5 knockout mouse cortex. Mechanistically, SEPTIN5 knockdown increases degradation of APP CTFs via the autophagosomal pathway, without affecting APP secretory trafficking or endocytosis, and enhances autophagosomal activity as indicated by altered autophagosomal marker levels. shRNA knockdown, Septin5 knockout mice, APP CTF and Aβ measurement by ELISA/Western blot, autophagy marker analysis, APP trafficking assay Cells High 33203136
2021 SEPTIN5 S327 phosphorylation status affects APP processing and autophagy markers in primary cortical neurons (assessed using lentiviral phosphomutants S327A and S327D). S327 phosphorylation status also influences short-term synaptic plasticity at the CA3-CA1 synapse ex vivo, linking this post-translational modification to synaptic function. Lentiviral transduction of primary mouse cortical neurons with wild-type SEPTIN5 and phosphomutants (S327A, S327D), APP processing assays, autophagy marker quantification, ex vivo electrophysiology (CA3-CA1) Neurobiology of disease Medium 34954322
2024 SEPTIN5 (CDCrel-1) interacts with VMAT2 in rat striatum, and binge methamphetamine alters this interaction as well as the subcellular localization of SEPTIN5. Co-immunoprecipitation from rat striatal tissue, subcellular fractionation, in vivo METH treatment model International journal of molecular sciences Medium 39684782
2024 Co-expression of Sept8-204 with SEPT5 induces formation of small vesicle-like structures that co-localize with synaptophysin. This vesicle-like structure and co-localization require palmitoylation of Sept8-204 (controlled by ZDHHC17/PPT1); loss of palmitoylation causes Sept8-204/SEPT5 to form large puncta that do not co-localize with synaptophysin. Fluorescence microscopy of co-expressed septins, palmitoylation inhibition (2-BP), ZDHHC17 and PPT1 knockouts, co-localization with synaptophysin marker Journal of cellular biochemistry Medium 38308620
2025 In pancreatic β-cells, SEPTIN5 is preferentially assembled at microtubule-plasma membrane contact sites in a microtubule-dependent manner, where it anchors secretory granules. Septin5 deletion destabilizes the cortical microtubule meshwork, increases insulin granule dynamics and access to the plasma membrane, increases releasable granule pool clustering on L-type Ca2+ channels, and dramatically enhances glucose-stimulated insulin secretion including in type 2 diabetes. Super-resolution imaging, Septin5 knockout rodent model, live-cell imaging of granule dynamics, Ca2+ channel co-localization analysis, insulin secretion assay in rodent and human islets Nature communications High 40108136
1998 SEPTIN5 (hCDCrel-1) protein localizes to neurons in adult human brain and co-purifies with synaptosomes marked by SNAP-25 and synaptophysin, indicating a presynaptic localization. Immunohistochemistry, subcellular fractionation/co-purification with synaptosomal markers Neuroreport Medium 9760144

Source papers

Stage 0 corpus · 42 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proceedings of the National Academy of Sciences of the United States of America 775 11078524
1999 The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nature neuroscience 316 10321247
2002 The septin CDCrel-1 is dispensable for normal development and neurotransmitter release. Molecular and cellular biology 105 11739749
2003 Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1. Proceedings of the National Academy of Sciences of the United States of America 94 14530399
2003 SEPT5_v2 is a parkin-binding protein. Brain research. Molecular brain research 88 14559152
2005 The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex. The Biochemical journal 81 15355307
2009 Sept5 deficiency exerts pleiotropic influence on affective behaviors and cognitive functions in mice. Human molecular genetics 69 19240081
2008 Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis. The Journal of neuroscience : the official journal of the Society for Neuroscience 61 18385322
2007 Targeted disruption of Sept3, a heteromeric assembly partner of Sept5 and Sept7 in axons, has no effect on developing CNS neurons. Journal of neurochemistry 58 17564677
2005 Neurotoxicity and behavioral deficits associated with Septin 5 accumulation in dopaminergic neurons. Journal of neurochemistry 55 16092945
2012 Alterations of social interaction through genetic and environmental manipulation of the 22q11.2 gene Sept5 in the mouse brain. Human molecular genetics 51 22589251
2004 Abnormalities of presynaptic protein CDCrel-1 in striatum of rats reared in social isolation: relevance to neural connectivity in schizophrenia. The European journal of neuroscience 49 15245502
2018 Autoimmune septin-5 cerebellar ataxia. Neurology(R) neuroimmunology & neuroinflammation 44 29998156
1998 Structure and expression of the human septin gene HCDCREL-1. Gene 43 9611266
1998 Localization of a novel septin protein, hCDCrel-1, in neurons of human brain. Neuroreport 39 9760144
2000 Characterization and expression analysis of two human septin genes, PNUTL1 and PNUTL2. Gene 38 11167005
2007 Phosphorylation of adult type Sept5 (CDCrel-1) by cyclin-dependent kinase 5 inhibits interaction with syntaxin-1. The Journal of biological chemistry 36 17224448
2011 Deletion of human GP1BB and SEPT5 is associated with Bernard-Soulier syndrome, platelet secretion defect, polymicrogyria, and developmental delay. Thrombosis and haemostasis 33 21800012
2002 Human septin-septin interaction: CDCrel-1 partners with KIAA0202. FEBS letters 27 12023038
2022 Septin-5 and -7-IgGs: Neurologic, Serologic, and Pathophysiologic Characteristics. Annals of neurology 23 36053822
2006 Human endothelial cell septins: SEPT11 is an interaction partner of SEPT5. The Journal of pathology 22 16767699
2019 miR-185 and SEPT5 Genes May Contribute to Parkinson's Disease Pathophysiology. Oxidative medicine and cellular longevity 20 31814881
2008 HSP70 and constitutively active HSF1 mediate protection against CDCrel-1-mediated toxicity. Molecular therapy : the journal of the American Society of Gene Therapy 19 18398426
2000 Reciprocal expression of infant- and adult-preferring transcripts of CDCrel-1 septin gene in the rat neocortex. Biochemical and biophysical research communications 19 10873671
2022 Downregulation of SEPTIN5 inhibits prostate cancer progression by increasing CD8+ T cell infiltration. International journal of biological sciences 17 36439885
2020 Presynaptic Vesicle Protein SEPTIN5 Regulates the Degradation of APP C-Terminal Fragments and the Levels of Aβ. Cells 14 33203136
2000 Expression of Cdcrel-1 (Pnutl1), a gene frequently deleted in velo-cardio-facial syndrome/DiGeorge syndrome. Mechanisms of development 13 10940632
2010 Ankyrin repeat-rich membrane spanning/Kidins220 protein interacts with mammalian Septin 5. Molecules and cells 12 20680483
2010 Neuronal expression of two isoforms of mouse Septin 5. Journal of neuroscience research 11 19937814
2007 Overexpression of Septin 4, the Drosophila homologue of human CDCrel-1, is toxic for dopaminergic neurons. The European journal of neuroscience 11 18028112
2021 S327 phosphorylation of the presynaptic protein SEPTIN5 increases in the early stages of neurofibrillary pathology and alters the functionality of SEPTIN5. Neurobiology of disease 10 34954322
2012 Septin 4, the drosophila ortholog of human CDCrel-1, accumulates in parkin mutant brains and is functionally related to the Nedd4 E3 ubiquitin ligase. Journal of molecular neuroscience : MN 10 22562816
2013 MLL-SEPT5 fusion transcript in infant acute myeloid leukemia with t(11;22)(q23;q11). Leukemia & lymphoma 9 23725386
2005 Immunoreactivity of the septins SEPT4, SEPT5, and SEPT8 in the human eye. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 9 15923366
2017 Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens. Proteomes 6 28895884
2018 Acute myeloid leukemia with KMT2A-SEPT5 translocation: A case report and review of the literature. SAGE open medical case reports 4 29326822
2021 MLL-SEPT5 Fusion Transcript in Myelodysplastic Syndrome Patient With t(11;22)(q23;q11). Frontiers in medicine 3 35004749
2014 Mixed lineage leukemia-septin 5 fusion transcript in de novo adult acute myeloid leukemia with t(11;22)(q23;q11.2): A case report. Oncology letters 3 24932261
2025 Septin5 deletion enhances β-cell exocytosis by releasing microtubule-tethered insulin granules onto plasma membrane. Nature communications 2 40108136
2024 Palmitoylation is required for Sept8-204 and Sept5 to form vesicle-like structure and colocalize with synaptophysin. Journal of cellular biochemistry 1 38308620
2026 Impairment of novelty-dependent hippocampal behavioural tagging in Septin5-deficient mice. Molecular brain 0 41634751
2024 Interactions of VMAT2 with CDCrel-1 and Parkin in Methamphetamine Neurotoxicity. International journal of molecular sciences 0 39684782

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