Affinage

SNAP29

Synaptosomal-associated protein 29 · UniProt O95721

Length
258 aa
Mass
29.0 kDa
Annotated
2026-06-10
58 papers in source corpus 36 papers cited in narrative 36 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

SNAP29 is a promiscuous SNAP-25-family t-SNARE that supplies the central QbQc-SNARE subunit for membrane fusion events across multiple intracellular trafficking pathways (PMID:11707603, PMID:11444821). Unlike the plasma-membrane-restricted SNAP-23, it binds both plasma-membrane and intracellular syntaxins with comparable affinity, and syntaxin binding augments its engagement of vesicle SNAREs, positioning it to serve many fusion steps (PMID:11444821). Its best-characterized role is driving autophagosome–lysosome fusion as the QbQc subunit of the STX17–SNAP29–VAMP8 fusogenic complex; VAMP8 displaces YKT6 from a priming STX17–SNAP29–YKT6 complex on autophagosomes to assemble the productive fusion machinery (PMID:38340317). SNAP29 also functions in ER-to-Golgi trafficking through complexes with Syntaxin5 (engaging SEC22B vesicles) and Syntaxin18 (PMID:33718375), in endocytic recycling of transferrin and beta1-integrin (PMID:20305790), and in synaptic vesicle recycling, where it acts as a negative modulator of neurotransmitter release by slowing SNARE complex disassembly (PMID:11707603, PMID:15890653). Beyond fusion, SNAP29 moonlights at the outer kinetochore, where it promotes Knl1 recruitment and faithful chromosome segregation (PMID:27647876). SNAP29 activity is tightly gated by post-translational modification: OGT-mediated O-GlcNAcylation inhibits SNARE complex formation and autophagic flux in a nutrient-dependent manner (PMID:25419848, PMID:36704963), NEK3 phosphorylation at S105 directs membrane association (PMID:29454964), and SNAP29 abundance and assembly are further controlled by caspase-3 cleavage at D30 (PMID:35670302), METTL3/YTHDF2-mediated m6A mRNA decay (PMID:40340690), and HRD1-regulated liquid-liquid phase separation that drives condensate-dependent SNARE assembly (PMID:41615796). Loss-of-function SNAP29 mutations cause CEDNIK syndrome, in which defective lamellar granule maturation and epidermal lipid/protease trafficking disrupt keratinocyte differentiation and the epidermal barrier (PMID:15968592, PMID:26747696).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2001 High

    Established SNAP29 as a SNARE-binding protein at synapses, defining its molecular identity and its role in regulating SNARE complex turnover rather than just fusion.

    Evidence Yeast two-hybrid against syntaxin-1A, Co-IP, synaptosomal fractionation, and presynaptic microinjection in neurons

    PMID:11707603

    Open questions at the time
    • Did not establish whether SNAP29 functions outside neurons
    • Direct fusion activity vs. disassembly inhibition not fully separated
  2. 2001 Medium

    Showed SNAP29 binds intracellular as well as plasma-membrane syntaxins (unlike SNAP-23), predicting a promiscuous role across multiple trafficking pathways.

    Evidence In vitro and in vivo binding assays with comparative SNAP-23 analysis

    PMID:11423532 PMID:11444821

    Open questions at the time
    • Which specific fusion events SNAP29 drives in vivo not resolved
    • Functional consequence of EHD1/AP-2 association on IGF-1R endocytosis not directly tested
  3. 2005 High

    Linked SNAP29 to a human Mendelian disease (CEDNIK) and to epidermal vesicle trafficking, demonstrating a non-redundant physiological requirement.

    Evidence Homozygosity mapping and sequencing of patients plus skin histology/EM and immunostaining

    PMID:15890653 PMID:15968592

    Open questions at the time
    • Molecular fusion step disrupted in keratinocytes not defined at this stage
    • Connection between trafficking defect and lamellar granule maturation mechanistic detail absent
  4. 2010 Medium

    Defined SNAP29 roles in endocytic recycling of transferrin and beta1-integrin using patient-derived cells, broadening its function beyond exocytic/synaptic fusion.

    Evidence CEDNIK patient fibroblast recycling, VSVG trafficking, and wound healing assays

    PMID:20305790

    Open questions at the time
    • No major exocytic defect detected, leaving pathway selectivity unexplained
    • Direct SNARE partners for recycling not identified
  5. 2011 Medium

    In vivo ortholog studies in C. elegans established SNAP29 requirements for secretion, endomembrane integrity, and recycling endosome morphology in a whole-organism context.

    Evidence C. elegans RNAi/mutant genetics with GFP-fusion localization and live imaging

    PMID:21545795 PMID:21613542

    Open questions at the time
    • Mammalian relevance of intestinal/secretory phenotypes uncertain
    • Specific cognate SNAREs for each compartment not mapped
  6. 2014 High

    Identified O-GlcNAcylation as a nutrient-responsive switch that inhibits SNAP29 SNARE complex assembly, establishing the first post-translational control of its fusogenic activity in autophagy.

    Evidence OGT knockdown, O-GlcNAc site mutagenesis, Co-IP, and autophagic flux assays in mammalian cells and C. elegans

    PMID:25419848

    Open questions at the time
    • Stoichiometry and exact O-GlcNAc sites partly inferred
    • Crosstalk with other SNAP29 modifications not addressed
  7. 2014 High

    Drosophila domain dissection demonstrated that both SNARE domains are required for SNAP29 function in autophagy, trafficking, and Golgi maintenance, separating SNARE activity from the NPF motif.

    Evidence Loss-of-function mutants with domain-mutant rescue, Co-IP, immunofluorescence, and EM

    PMID:24626111 PMID:25551675

    Open questions at the time
    • Why some Drosophila complexes are not SDS-resistant unresolved
    • Relative contributions of autophagy vs. general trafficking to phenotype not separated
  8. 2016 High

    Revealed a moonlighting role at the outer kinetochore, where SNAP29 promotes Knl1 recruitment, decoupling a fusion SNARE from chromosome segregation.

    Evidence Drosophila and human cell RNAi, immunofluorescence localization, segregation assays, and point mutagenesis

    PMID:27647876

    Open questions at the time
    • How a SNARE protein is recruited to kinetochores mechanistically unclear
    • Whether SNARE-binding and kinetochore functions compete in vivo not quantified
  9. 2018 Medium

    Established NEK3-mediated S105 phosphorylation as a determinant of SNAP29 membrane association, adding a second regulatory layer governing its localization and recycling function.

    Evidence Kinase assay, S105A mutagenesis, Co-IP, and rescue in CEDNIK patient fibroblasts

    PMID:29454964

    Open questions at the time
    • Interplay between phosphorylation and O-GlcNAcylation not tested
    • Membrane targeting mechanism downstream of S105 not defined
  10. 2018 High

    Connected pathological O-GlcNAcylation of SNAP29 to autophagy failure in arsenic toxicity and diabetic cardiomyopathy, validating the modification as a disease-relevant brake on STX17-SNAP29-VAMP8 assembly.

    Evidence CRISPR KO rescue with O-GlcNAc-defective mutant, SNARE Co-IP, and in vivo diabetic/arsenic models

    PMID:29507186 PMID:30221662

    Open questions at the time
    • Tissue-specific OGT regulation of SNAP29 not fully mapped
    • Reversibility kinetics in vivo not measured
  11. 2019 High

    First vertebrate (zebrafish and mouse) genetic models recapitulated CEDNIK with autophagy marker accumulation, multilamellar organelle defects, and neuronal phenotypes, unifying the trafficking and autophagy roles in disease.

    Evidence Zebrafish mutants and conditional/total Snap29 knockout mice with EM, immunofluorescence, and western blotting

    PMID:26747696 PMID:30718891

    Open questions at the time
    • Causal contribution of autophagy vs. recycling defects to skin/neural phenotype not separated
    • ER stress origin not mechanistically traced to a single fusion step
  12. 2021 Medium

    Defined SNAP29 complexes with Syntaxin5 and Syntaxin18 at the ER/Golgi engaging SEC22B vesicles, establishing a direct role in ER-to-Golgi trafficking distinct from autophagy.

    Evidence Co-IP, live imaging across HeLa, neuroepithelial cells, and in vivo Drosophila trafficking assays

    PMID:33718375

    Open questions at the time
    • Which vesicle R-SNARE completes each ER/Golgi complex not fully defined
    • Regulation of pathway choice between Golgi and autophagic SNAREs unknown
  13. 2022 Medium

    Identified additional regulatory inputs (caspase-3 cleavage at D30 by viral ORF7a; syntaxin6-dependent GLUT4 vesicle sequestration), expanding SNAP29 control into innate immunity and metabolic signaling.

    Evidence Caspase cleavage site identification with autophagy assays; mass spectrometry, Co-IP, and GLUT4 translocation/glucose uptake assays

    PMID:35670302 PMID:36181414

    Open questions at the time
    • Whether D30 cleavage occurs under physiological conditions unclear
    • GLUT4 anchoring vs. trafficking dual role not mechanistically reconciled
  14. 2024 High

    Resolved the assembly order of the autophagic fusion machinery, showing YKT6 primes a STX17-SNAP29 complex that VAMP8 converts into the fusogenic form, refining how SNAP29 templates membrane fusion.

    Evidence Co-IP, in vitro reconstitution with lipid mixing, and autophagy flux assays

    PMID:38340317 PMID:39283311

    Open questions at the time
    • What governs the YKT6-to-VAMP8 handoff in vivo not defined
    • Migfilin's structural role in promoting assembly not resolved at atomic level
  15. 2025 Medium

    Established that SNAP29 forms HRD1-regulated dynamic condensates and is controlled by m6A mRNA decay and lysine lactylation, framing phase separation and turnover as additional determinants of SNARE assembly capacity.

    Evidence In vitro/in vivo LLPS reconstitution with HRD1 KO; MeRIP/RIP-qPCR with AAV rescue; CHX chase for lactylation-driven degradation

    PMID:40340690 PMID:41615796 PMID:41975562

    Open questions at the time
    • Lactylation mechanism described with limited structural detail (Low-confidence finding)
    • How condensation, modification, and complex assembly are integrated remains unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • A unifying model for how SNAP29's many regulatory inputs (O-GlcNAcylation, phosphorylation, lactylation, m6A decay, cleavage, ubiquitination, and phase separation) are coordinated to select among its diverse fusion and non-fusion functions remains unestablished.
  • No integrated structural or quantitative model of competing modifications
  • Mechanism directing SNAP29 between autophagy, Golgi, recycling, and kinetochore roles unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0008092 cytoskeletal protein binding 1 GO:0140313 molecular sequestering activity 1
Localization
GO:0005768 endosome 3 GO:0005886 plasma membrane 3 GO:0005794 Golgi apparatus 2 GO:0005783 endoplasmic reticulum 1 GO:0005815 microtubule organizing center 1 GO:0005829 cytosol 1
Pathway
R-HSA-9612973 Autophagy 4 R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-9609507 Protein localization 3 R-HSA-112316 Neuronal System 2 R-HSA-1640170 Cell Cycle 1
Partners
EHD1NEK3OGTSTX17STX18STX5VAMP8YKT6
Complex memberships
STX17-SNAP29-VAMP8 SNARE complexSTX17-SNAP29-YKT6 priming complexSTX5-SNAP29 (SEC22B) ER-Golgi complexouter kinetochore

Evidence

Reading pass · 36 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 SNAP-29 was isolated as a syntaxin-1A-binding protein via yeast two-hybrid from human brain cDNA; it localizes to synaptic vesicles in hippocampal neurons, competes with alpha-SNAP for binding to synaptic SNAREs, and inhibits SNARE complex disassembly, reducing synaptic transmission in an activity-dependent manner when introduced into presynaptic neurons. Yeast two-hybrid, immunoprecipitation, synaptosomal fractionation, immunocytochemistry, presynaptic microinjection in SCG neurons Proceedings of the National Academy of Sciences of the United States of America High 11707603
2001 SNAP-29 binds both plasma membrane and intracellular syntaxins equally well (unlike SNAP-23 which prefers plasma membrane syntaxins), and syntaxin binding to SNAP-29 augments vesicle SNARE binding; this 'promiscuous' binding suggests SNAP-29 functions in multiple intracellular protein trafficking pathways. In vitro and in vivo binding assays (pull-down, co-IP), comparative binding studies with SNAP-23 Biochemical and biophysical research communications Medium 11444821
2001 SNAP29 interacts directly with EHD1 and both co-localize in endocytic vesicles and form complexes with alpha-adaptin of AP-2; both proteins are present in complexes with IGF-1R, implicating SNAP29 in IGF-1R endocytosis. Co-immunoprecipitation, co-localization by immunofluorescence, yeast two-hybrid The Journal of biological chemistry Medium 11423532
2005 Loss-of-function mutation (1-bp deletion) in SNAP29 causes CEDNIK syndrome; decreased SNAP29 expression results in abnormal lamellar granule maturation, mislocation of epidermal lipids and proteases, establishing SNAP29 as essential for vesicle-mediated epidermal differentiation. Homozygosity mapping, sequencing, patient skin histology/EM, immunostaining American journal of human genetics High 15968592
2005 Exogenous SNAP-29 in presynaptic hippocampal neurons decreases synaptic transmission efficiency during repetitive firing at low-moderate frequencies and impairs recovery after synaptic depression; knockdown of SNAP-29 by siRNA increases synaptic transmission efficiency, acting as a negative modulator of neurotransmitter release by slowing SNARE recycling. Dual patch-clamp whole-cell recording, FM dye imaging, immunocytochemistry, siRNA knockdown The Journal of biological chemistry High 15890653
2009 SNAP-29 interacts with GTPases Rab3A (GTP-dependently), Rab24, and septin 4 via its N-terminal domain; Rab3A co-expression redistributes cytoplasmic SNAP-29 pools and enhances surface-directed trafficking of myelin proteolipid protein, suggesting Rab3A regulates SNAP-29-mediated membrane fusion. Yeast two-hybrid, co-immunoprecipitation, co-localization, HEK293 overexpression trafficking assay Journal of neuroscience research Medium 19170188
2010 SNAP29 mediates endocytic recycling of transferrin and beta1-integrin; impaired beta1-integrin recycling in CEDNIK patient fibroblasts (SNAP29-deficient) causes defective cell spreading and wound healing. No major defect in exocytosis of VSVG from Golgi was detected, but Golgi morphology was dispersed. Patient-derived fibroblasts, transferrin recycling assay, beta1-integrin recycling assay, VSVG trafficking assay, wound healing assay PloS one Medium 20305790
2011 In C. elegans, SNAP-29 depletion causes endomembrane fragmentation, blocks yolk secretion, and disrupts apical and basolateral plasma membrane protein targeting in intestinal cells; functional SNAP-29::GFP localizes mainly to plasma membrane and late Golgi and partially to endosomes. C. elegans RNAi, fluorescent protein tagging, live imaging, genetic analysis Molecular biology of the cell Medium 21613542
2011 A novel homozygous insertion in SNAP29 (c.486insA) causes CEDNIK syndrome; in vitro transfection confirms loss-of-function; 3D keratinocyte organotypic cultures with SNAP29 knockdown replicate CEDNIK histological features, establishing SNAP29 as essential for epidermal differentiation machinery. Sequencing, in vitro mutagenesis, transfection assays, 3D organotypic keratinocyte cultures with SNAP29 knockdown The British journal of dermatology Medium 21073448
2011 C. elegans snap-29 is required for oocyte maturation, embryonic cytokinesis, and basolateral/apical intestinal secretion; SNAP-29::GFP is enriched on recycling endosomes; loss of SNAP-29 disrupts recycling endosome morphology, indicating a role in fusion of post-Golgi vesicles with recycling endosomes. C. elegans genetics (RNAi, mutants), GFP fusion localization, fluorescence microscopy Developmental biology Medium 21545795
2012 SNAP29 is localized in the endocytic pathway of mast cells and is transiently recruited to E. coli-containing phagosomes; overexpression of SNAP29 significantly increases internalization and killing of E. coli without affecting exocytosis of inflammatory mediators. Immunofluorescence localization, SNAP29 overexpression, bacterial internalization/killing assay in mast cells PloS one Medium 23185475
2014 OGT mediates O-GlcNAcylation of SNAP-29, inhibiting formation of the SNAP-29-containing SNARE complex; OGT knockdown or mutation of O-GlcNAc sites in SNAP-29 promotes SNARE complex formation, increases autophagosome-endosome/lysosome fusion, and promotes autophagic flux in a nutrient-dependent manner in mammalian cells and C. elegans. OGT knockdown, O-GlcNAc site mutagenesis, co-immunoprecipitation, autophagic flux assays, C. elegans genetics Nature cell biology High 25419848
2014 Drosophila Snap29 contains two SNARE domains and an NPF motif; both SNARE domains are required for function (NPF motif is partially dispensable); Snap29 interacts with SNARE proteins, localizes to multiple trafficking organelles, and is required for autophagy, protein trafficking, and Golgi morphology; loss causes epithelial architecture defects linked to elevated Hop-Stat92E signaling. Drosophila loss-of-function mutants, rescue experiments with domain mutants, co-immunoprecipitation, immunofluorescence, electron microscopy Autophagy High 25551675
2014 Drosophila SNAP-29 (dSNAP-29) interacts with dsyntaxin1 and dsyntaxin16 in vitro but does not form SDS-resistant SNARE complexes; it associates with EH domain-containing proteins at the plasma membrane and in intracellular puncta, implicating it in the endocytic pathway. In vitro binding assays, SDS-PAGE SNARE complex assay, immunofluorescence, RNAi/overexpression in Drosophila PloS one Medium 24626111
2015 Snap29 knockout mice (total and keratinocyte-specific) display ichthyosis, acanthosis, hyperkeratosis, abnormal keratinocyte differentiation, impaired epidermal barrier, malformed lamellar bodies with decreased deposition of contents, increased LC3-II levels (autophagy defect), and ER stress marker induction. Conditional/total Snap29 knockout mouse models, histology, electron microscopy, western blotting, immunofluorescence The Journal of investigative dermatology High 26747696
2016 Snap29 localizes to the outer kinetochore in Drosophila and human cells and promotes kinetochore assembly by mediating Knl1 recruitment; loss of Snap29 causes chromosome mis-segregation and fragmented nuclei. A Snap29 point mutant that blocks release from SNARE fusion complexes causes ectopic Knl1 recruitment to trafficking compartments. Drosophila genetics, human cell RNAi, immunofluorescence localization, chromosome segregation assays, point mutagenesis The EMBO journal High 27647876
2018 Arsenic exposure blocks autophagosome-lysosome fusion by disrupting STX17-SNAP29-VAMP8 SNARE complex formation, at least in part via enhancing O-GlcNAcylation of SNAP29; CRISPR SNAP29 knockout cells transfected with O-GlcNAcylation-defective SNAP29 (but not wild-type) abolished arsenic-mediated autophagy inhibition. CRISPR knockout, rescue with mutant SNAP29, Co-IP of SNARE complex, autophagic flux assays Molecular and cellular biology High 29507186
2018 NEK3 kinase phosphorylates SNAP29 at serine 105 (S105); this phosphorylation directs SNAP29 membrane association; S105A phosphorylation-defective mutant causes defective focal adhesion formation, impaired Golgi structure, and attenuated cellular recycling, whereas wild-type SNAP29 partially rescues CEDNIK patient fibroblast morphology. Kinase assay, site-directed mutagenesis, co-immunoprecipitation, immunofluorescence in patient fibroblasts Biochemical and biophysical research communications Medium 29454964
2018 O-GlcNAc modification of SNAP29 in type I diabetic rat hearts inhibits STX17-SNAP29-VAMP8 SNARE complex formation, thereby blocking autophagic flux and exacerbating myocardial injury; co-immunoprecipitation confirmed the disrupted complex under high O-GlcNAc conditions. Streptozotocin rat model, thiamet G/DON pharmacological tools, co-immunoprecipitation, echocardiography, cardiomyocyte culture International journal of molecular medicine Medium 30221662
2019 Zebrafish snap29 homozygous mutants display CEDNIK-like features (microcephaly, skin defects), accumulate autophagy markers p62 and LC3, form aberrant multilamellar organelles and mitochondria, exhibit high apoptosis, and show defective trigeminal nerve formation with excess axonal branching. Zebrafish snap29 mutant genetic model, electron microscopy, immunofluorescence, confocal imaging Scientific reports High 30718891
2019 DAPK3 regulates autophagy; silencing DAPK3 decreases assembly of the STX17-SNAP29-VAMP8 complex, leading to blockade of autophagosome-lysosome fusion by mediating SNAP29. DAPK3 siRNA knockdown, Co-IP of STX17-SNAP29-VAMP8 complex, autophagic flux assays in trophoblast cells Molecular and cellular endocrinology Low 31811899
2020 SNAP29 mediates assembly of histidine-induced CTPS filaments along the cytokeratin network in a KRT8-dependent manner; knockdown of SNAP29 interferes with CTPS filament assembly and relieves filament-induced suppression of CTPS enzymatic activity; APEX2 proximity labeling identified SNAP29 association with cytokeratin under stress. CTPS-APEX2 proximity labeling, SNAP29 knockdown, super-resolution imaging, co-localization with cytokeratin network Journal of cell science Medium 32184263
2020 TNFα reduces SNAP29 expression via NF-κB–FOXP3 axis (FOXP3 is confirmed as a transcription factor for SNAP29 by promoter binding assay), thereby impairing autophagosome-lysosome fusion and increasing prion protein level to promote tumor cell migration. SNAP29 knockdown, promoter binding assay for FOXP3, NF-κB pathway analysis, cell migration assay Virologica Sinica Medium 33237393
2021 SNAP29 forms a complex with Syntaxin18 or Syntaxin5 at the ER and Golgi apparatus; the Syntaxin5-SNAP29 complex engages SEC22B-loaded vesicles; decreased SNAP29 activity alters Golgi architecture and reduces ER-to-Golgi trafficking in HeLa cells, neuroepithelial stem cells, and in vivo. Co-immunoprecipitation, live imaging in HeLa and neuroepithelial cells, in vivo Drosophila analysis, trafficking assays Frontiers in cell and developmental biology Medium 33718375
2021 Alpha-Synuclein overexpression decreases SNAP29 protein abundance, compromising autophagosome-lysosome fusion and reducing autolysosome formation; SNAP29 knockdown mimics alpha-Syn effects; SNAP29 co-expression reverses alpha-Syn-induced autophagy changes and ameliorates dopaminergic neuronal cell death. SNAP29 knockdown and overexpression, LC3/autophagy flux assays, extracellular vesicle analysis, human post-mortem brain immunostaining Cell death & disease Medium 34535638
2022 SARS-CoV-2 ORF7a activates CASP3 (caspase 3), which cleaves SNAP29 at aspartic acid residue D30, impairing autophagosome-lysosome fusion and blocking autophagic flux, thereby promoting autophagosome accumulation and viral replication. ORF7a overexpression, shRNA knockdown, caspase 3 cleavage assay, autophagy flux assays, SNAP29 cleavage site identification Autophagy Medium 35670302
2022 SNAP29 sequesters and anchors GLUT4-containing vesicles in the perinuclear insulin-responsive compartment (IRC) of adipocytes by binding syntaxin6; SNAP29 overexpression aggregates GLUT4 vesicles perinuclearly while silencing disperses them; both conditions inhibit insulin-stimulated glucose uptake. Mass spectrometry identification, co-immunoprecipitation, immunofluorescence, GLUT4 translocation assay, glucose uptake assay in 3T3-L1 adipocytes Journal of diabetes investigation Medium 36181414
2023 OGT-mediated O-GlcNAcylation of SNAP29 blocks autophagosome-lysosome fusion by inhibiting SNARE fusion complex formation; SM15 compound enhances SNAP29 O-GlcNAcylation; genetic or pharmacological OGT inhibition or O-GlcNAcylation-defective SNAP29 mutant rescues autophagic flux, ROS production, and apoptosis. Biochemical autophagic flux assays, OGT inhibition/knockdown, O-GlcNAcylation-defective SNAP29 mutant expression, SNARE complex immunoprecipitation Autophagy High 36704963
2023 PRRSV nsp5 interacts with STX17 (but not SNAP29) and inhibits the STX17-SNAP29 interaction, impairing STX17-SNAP29-VAMP8 SNARE complex assembly and autophagosome-lysosome fusion. Co-immunoprecipitation, domain mapping, autophagy flux assays in PRRSV-infected and nsp5-overexpressing cells Microbiology spectrum Medium 36815765
2024 YKT6 forms a priming complex with STX17 and SNAP29 on autophagosomes via its SNARE domain; VAMP8 displaces YKT6 to form the fusogenic STX17-SNAP29-VAMP8 complex; the YKT6-SNAP29-STX17 complex facilitates lipid and content mixing driven by STX17-SNAP29-VAMP8, indicating a priming role. Co-immunoprecipitation, in vitro reconstitution/lipid mixing assays, autophagy flux assays Cell reports High 38340317
2024 Migfilin associates with SNAP29 and VAMP8, facilitating STX17-SNAP29-VAMP8 SNARE complex assembly; migfilin depletion disrupts SNAP29-mediated SNARE complex formation, blocks autophagosome-lysosome fusion, and suppresses cancer cell growth; SNARE complex reassembly rescues these defects. Co-immunoprecipitation, SNARE complex assembly assay, autophagy flux assays, migfilin depletion in cancer cells The Journal of cell biology Medium 39283311
2023 RUNDC1 clasps the ATG14-STX17-SNAP29 complex by stimulating ATG14 homo-oligomerization, inhibiting ATG14 dissociation and preventing VAMP8 from binding STX17-SNAP29; phosphorylation of RUNDC1 Ser379 is crucial for this inhibition of STX17-SNAP29-VAMP8 complex assembly. Co-immunoprecipitation, gain/loss-of-function studies in human cells and zebrafish, phosphorylation site mutagenesis Cell death and differentiation Medium 37684417
2025 METTL3-mediated m6A methylation of SNAP29 mRNA promotes its degradation via YTHDF2, reducing SNAP29 protein levels in ischemic flaps; SNAP29 deficiency disrupts autophagic flux and increases ROS-induced parthanatos; AAV-mediated SNAP29 restoration reversed these effects in vivo. RIP-qPCR, MeRIP-qPCR, RNA stability assays, AAV rescue in vivo, western blotting, immunofluorescence, proteomics Autophagy Medium 40340690
2025 Lactate-induced lysine lactylation of SNAP29 at K169 promotes its degradation, impairing autophagic flux and trophoblast function in the context of senescence-associated metabolic dysregulation. Western blotting, immunofluorescence, CHX chase (protein stability), in vitro and in vivo trophoblast models Autophagy Low 41975562
2026 HRD1 (E3 ubiquitin ligase) interacts with SNAP29 and suppresses its liquid-liquid phase separation (LLPS); HRD1 deficiency accelerates SNAP29 condensate formation and SNARE complex assembly, promoting autolysosome formation; SNAP29 forms highly dynamic condensates in vivo and in vitro that are crucial for SNARE complex assembly. Co-immunoprecipitation, in vivo and in vitro condensate/LLPS assays, HRD1 knockout, SNAP29-dependent autophagy assays Cell reports Medium 41615796
2025 Legionella SidE effectors mediate phosphoribosyl ubiquitination (PR-Ub) of SNAP29; PR-Ub of SNAP29 inhibits formation of the autophagosomal SNARE complex (STX17-SNAP29-VAMP8) by steric hindrance, preventing fusion of bacterial vacuoles with lysosomes. Proximity labeling, mass spectrometry identification of PR-Ub sites, mutational studies, biochemical complex assays, Legionella infection model bioRxivpreprint Medium bio_10.1101_2025.05.19.654886

Source papers

Stage 0 corpus · 58 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation. Nature cell biology 245 25419848
2005 A mutation in SNAP29, coding for a SNARE protein involved in intracellular trafficking, causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma. American journal of human genetics 150 15968592
2022 The ORF7a protein of SARS-CoV-2 initiates autophagy and limits autophagosome-lysosome fusion via degradation of SNAP29 to promote virus replication. Autophagy 108 35670302
2001 Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29. The Journal of biological chemistry 108 11423532
2012 Hemizygous mutations in SNAP29 unmask autosomal recessive conditions and contribute to atypical findings in patients with 22q11.2DS. Journal of medical genetics 90 23231787
2021 Alpha-Synuclein defects autophagy by impairing SNAP29-mediated autophagosome-lysosome fusion. Cell death & disease 84 34535638
2014 Multiple functions of the SNARE protein Snap29 in autophagy, endocytic, and exocytic trafficking during epithelial formation in Drosophila. Autophagy 77 25551675
2011 CEDNIK syndrome results from loss-of-function mutations in SNAP29. The British journal of dermatology 75 21073448
2001 SNAP-29: a general SNARE protein that inhibits SNARE disassembly and is implicated in synaptic transmission. Proceedings of the National Academy of Sciences of the United States of America 73 11707603
2005 SNAP-29-mediated modulation of synaptic transmission in cultured hippocampal neurons. The Journal of biological chemistry 69 15890653
2001 SNAP-29 is a promiscuous syntaxin-binding SNARE. Biochemical and biophysical research communications 59 11444821
2010 Loss of SNAP29 impairs endocytic recycling and cell motility. PloS one 55 20305790
2023 Blockage of autophagosome-lysosome fusion through SNAP29 O-GlcNAcylation promotes apoptosis via ROS production. Autophagy 50 36704963
2011 Caenorhabditis elegans SNAP-29 is required for organellar integrity of the endomembrane system and general exocytosis in intestinal epithelial cells. Molecular biology of the cell 50 21613542
2009 The SNARE protein SNAP-29 interacts with the GTPase Rab3A: Implications for membrane trafficking in myelinating glia. Journal of neuroscience research 46 19170188
2018 Increased O-GlcNAcylation of SNAP29 Drives Arsenic-Induced Autophagic Dysfunction. Molecular and cellular biology 42 29507186
2018 O-GlcNAc-modified SNAP29 inhibits autophagy-mediated degradation via the disturbed SNAP29-STX17-VAMP8 complex and exacerbates myocardial injury in type I diabetic rats. International journal of molecular medicine 41 30221662
2001 Polymorphism in SNAP29 gene promoter region associated with schizophrenia. Molecular psychiatry 39 11317222
2025 METTL3-dependent m6A modification of SNAP29 induces "autophagy-mitochondrial crisis" in the ischemic microenvironment after soft tissue transplantation. Autophagy 35 40340690
2015 Establishment of Two Mouse Models for CEDNIK Syndrome Reveals the Pivotal Role of SNAP29 in Epidermal Differentiation. The Journal of investigative dermatology 29 26747696
2024 Human YKT6 forms priming complex with STX17 and SNAP29 to facilitate autophagosome-lysosome fusion. Cell reports 26 38340317
2018 How to use a multipurpose SNARE: The emerging role of Snap29 in cellular health. Cell stress 26 31225470
2011 Essential roles of snap-29 in C. elegans. Developmental biology 26 21545795
2022 Apicoplast biogenesis mediated by ATG8 requires the ATG12-ATG5-ATG16L and SNAP29 complexes in Toxoplasma gondii. Autophagy 24 36095096
2012 A novel function for SNAP29 (synaptosomal-associated protein of 29 kDa) in mast cell phagocytosis. PloS one 24 23185475
2011 Abca12-mediated lipid transport and Snap29-dependent trafficking of lamellar granules are crucial for epidermal morphogenesis in a zebrafish model of ichthyosis. Disease models & mechanisms 23 21816950
2023 Porcine Reproductive and Respiratory Syndrome Virus nsp5 Induces Incomplete Autophagy by Impairing the Interaction of STX17 and SNAP29. Microbiology spectrum 21 36815765
2019 A genetic model of CEDNIK syndrome in zebrafish highlights the role of the SNARE protein Snap29 in neuromotor and epidermal development. Scientific reports 20 30718891
2019 Silencing DAPK3 blocks the autophagosome-lysosome fusion by mediating SNAP29 in trophoblast cells under high glucose treatment. Molecular and cellular endocrinology 20 31811899
2023 RUNDC1 inhibits autolysosome formation and survival of zebrafish via clasping ATG14-STX17-SNAP29 complex. Cell death and differentiation 19 37684417
2019 Compound heterozygous mutations in SNAP29 is associated with Pelizaeus-Merzbacher-like disorder (PMLD). Human genetics 16 31748968
2017 CEDNIK: Phenotypic and Molecular Characterization of an Additional Patient and Review of the Literature. Child neurology open 16 29051910
2016 An essential step of kinetochore formation controlled by the SNARE protein Snap29. The EMBO journal 16 27647876
2024 The crustacean DNA virus tegument protein VP26 binds to SNAP29 to inhibit SNARE complex assembly and autophagic degradation. Journal of virology 14 38189252
2021 Activity of the SNARE Protein SNAP29 at the Endoplasmic Reticulum and Golgi Apparatus. Frontiers in cell and developmental biology 14 33718375
2020 SNAP29 mediates the assembly of histidine-induced CTP synthase filaments in proximity to the cytokeratin network. Journal of cell science 13 32184263
2019 Snap29 mutant mice recapitulate neurological and ophthalmological abnormalities associated with 22q11 and CEDNIK syndrome. Communications biology 12 31633066
2014 Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic. PloS one 12 24626111
2023 Inhibition of STX17-SNAP29-VAMP8 complex formation by costunolide sensitizes ovarian cancer cells to cisplatin via the AMPK/mTOR signaling pathway. Biochemical pharmacology 11 37060961
2021 New Cohort of Patients With CEDNIK Syndrome Expands the Phenotypic and Genotypic Spectra. Neurology. Genetics 11 33977139
2015 Identification of roles for the SNARE-associated protein, SNAP29, in mouse platelets. Platelets 10 26587753
2020 Tumor Necrosis Factor α Reduces SNAP29 Dependent Autolysosome Formation to Increase Prion Protein Level and Promote Tumor Cell Migration. Virologica Sinica 9 33237393
2019 CEDNIK syndrome in an Indian patient with a novel mutation of the SNAP29 gene. Pediatric dermatology 8 30793783
2018 NEK3-mediated SNAP29 phosphorylation modulates its membrane association and SNARE fusion dependent processes. Biochemical and biophysical research communications 8 29454964
2022 Snapshots from within the cell: Novel trafficking and non trafficking functions of Snap29 during tissue morphogenesis. Seminars in cell & developmental biology 7 35256275
2021 Generation and Characterization of a CRISPR/Cas9-Mediated SNAP29 Knockout in Human Fibroblasts. International journal of molecular sciences 7 34069872
2024 Migfilin promotes autophagic flux through direct interaction with SNAP29 and Vamp8. The Journal of cell biology 4 39283311
2022 SNARE-binding protein synaptosomal-associated protein of 29 kDa (SNAP29) regulates the intracellular sequestration of glucose transporter 4 (GLUT4) vesicles in adipocytes. Journal of diabetes investigation 3 36181414
2022 CEDNIK syndrome in a Brazilian patient with compound heterozygous pathogenic variants. European journal of medical genetics 2 35093605
2022 CEDNIK syndrome with phenotypic variability. Pediatric dermatology 2 35229899
2025 purpleoid , a classic Drosophila eye color mutation, is an allele of the t-SNARE-encoding gene SNAP29. microPublication biology 1 40270683
2023 Snap29 Is Dispensable for Self-Renewal Maintenance but Required for Proper Differentiation of Mouse Embryonic Stem Cells. International journal of molecular sciences 1 36614195
2026 HRD1 negatively regulates autolysosome formation by inhibiting liquid-liquid phase separation of SNAP29. Cell reports 0 41615796
2026 Z-Guggulsterone Inhibits Triple-Negative Breast Cancer Progression by Blocking Autophagosome-Lysosome Fusion via OGT-Mediated SNAP29 O-GlcNAcylation. Phytotherapy research : PTR 0 41684288
2026 Trophoblast aging driven by IL33 deficiency elevates recurrent pregnancy loss risk through SNAP29 lactylation-mediated autophagy impairment. Autophagy 0 41975562
2025 Corrigendum to "STING guides the STX17-SNAP29-VAMP8 complex assembly to control autophagy" [Cell Insight 3 (2024) 100147]. Cell insight 0 40256202
2025 Expanded Phenotypic Spectrum of Cerebral Dysgenesis, Neuropathy, Ichthyosis, and Keratoderma (CEDNIK) Syndrome: A Rare Case Featuring Supraventricular Tachycardia and Tethered Spinal Cord. Cureus 0 40709160
2024 Pyloric Stenosis in a Patient with CEDNIK Syndrome. Cureus 0 38826968

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