| 2000 |
Syntaxin 7 localizes to late endosomes/lysosomes and associates with VAMP8 (Vamp 8) by co-immunoprecipitation; syntaxin 7 is specifically required for fusion of late endosomes with lysosomes in vitro, identifying a SNARE complex (syntaxin 7 / VAMP8) that functions in the late endocytic pathway. |
Co-immunoprecipitation, cell-free in vitro fusion assay, immunolocalization |
Molecular biology of the cell |
High |
10982406
|
| 2001 |
In B16 melanoma cells, immunoaffinity purification of syntaxin 7 co-isolated VAMP8 and VAMP7 among other SNARE partners (syntaxin 6, mVti1b, αSNAP), suggesting that syntaxin 7/mVti1b/syntaxin 6 can form discrete complexes with either VAMP7 or VAMP8 to regulate late endosomal fusion events. |
Large-scale immunoaffinity purification, electrospray mass spectrometry, immunoblotting, co-immunoprecipitation, confocal colocalization |
The Journal of biological chemistry |
Medium |
11278762
|
| 2004 |
In antibody-inhibition experiments using rat liver cell-free systems, the Q-SNARE complex of syntaxin 7/Vti1b/syntaxin 8 plus VAMP8 mediates homotypic late-endosome fusion, while the same Q-SNAREs combine with VAMP7 for heterotypic late-endosome–lysosome fusion; separate co-immunoprecipitation confirmed distinct syntaxin 7 complexes with VAMP7 vs. VAMP8 in solubilized liver membranes. |
Antibody inhibition in cell-free fusion assay, co-immunoprecipitation, overexpression of VAMP7 N-terminal domain to inhibit heterotypic fusion |
EMBO reports |
High |
15133481
|
| 2004 |
VAMP8 is enriched on zymogen granule membranes in pancreatic acinar cells and forms a SNARE complex with syntaxin 4 and SNAP-23. VAMP8-knockout mice accumulate zymogen granules (~3-fold) and show abolished secretagogue-stimulated exocytosis from acinar cells, establishing VAMP8 as the major v-SNARE for regulated exocytosis in exocrine pancreas. |
Targeted gene knockout in mice, immunohistochemistry, co-immunoprecipitation, secretion assay from pancreatic fragments |
Developmental cell |
High |
15363411
|
| 2006 |
VAMP8 (endobrevin) is the primary v-SNARE for platelet dense-core granule, alpha-granule, and lysosome release; VAMP8-/- mouse platelets show significant agonist-induced secretion defects, while VAMP-2+/-, VAMP-3-/-, and VAMP-2+/-/VAMP-3-/- platelets show no defect. Tetanus toxin (cleaving VAMP-2/-3) blocks residual release in VAMP-8-/- platelets, revealing a secondary role for VAMP-2/-3. |
Genetic knockout (VAMP-8-/-, VAMP-2+/-, VAMP-3-/-) platelet secretion assays, tetanus toxin treatment of permeabilized platelets |
Molecular biology of the cell |
High |
17065550
|
| 2002 |
VAMP-3 and VAMP-8 (but not VAMP-1 or VAMP-2) are identified in human platelets by mass spectrometry co-immunoprecipitated with syntaxin 4; recombinant VAMP-8 added to permeabilized platelets inhibits dense-granule secretion but not alpha-granule secretion, while rVAMP-3 inhibits both, demonstrating isoform-specific roles in platelet exocytosis. |
Nano-ESI tandem MS, immunoblotting, co-immunoprecipitation with syntaxin 4, competitive inhibition assay with recombinant VAMPs in permeabilized platelets |
Blood |
High |
12130530
|
| 2007 |
VAMP8 is expressed in all examined exocrine tissues (salivary, lacrimal, sweat, sebaceous, mammary glands, prostate). VAMP8-null mice show severe secretory granule accumulation and impaired pilocarpine-stimulated secretion in salivary and lacrimal glands; VAMP8 co-immunoprecipitates with syntaxin 4 and SNAP-23, establishing it as a general v-SNARE for regulated exocrine secretion. |
VAMP8-null mouse phenotyping, immunohistochemistry, electron microscopy, stimulated secretion assay, co-immunoprecipitation |
Molecular biology of the cell |
High |
17215514
|
| 2007 |
In permeabilized rat basophilic leukaemia cells, recombinant VAMP8/endobrevin (but not other R-SNAREs tested) specifically blocks hexosaminidase exocytosis; this secretion is insensitive to clostridial neurotoxins, consistent with VAMP8 serving as the primary R-SNARE for mast cell granule exocytosis. |
Permeabilized cell exocytosis inhibition assay with complete set of recombinant mammalian R-SNAREs, hexosaminidase release assay, clostridial neurotoxin treatment |
FEBS letters |
High |
17618625
|
| 2008 |
In bone marrow-derived mast cells, VAMP-8 co-localizes with secretory granules and redistributes upon stimulation, forming increased SNARE complexes with SNAP-23 and syntaxin-4. VAMP-8-deficient BMMCs show markedly reduced degranulation after IgE/antigen, thapsigargin, or ionomycin stimulation; plasma histamine is reduced in passive systemic anaphylaxis in VAMP-8-/- mice. Cytokine/chemokine release is not affected, while unprocessed TNF accumulates at the plasma membrane in a VAMP-3-positive compartment, demonstrating that VAMP-8 segregates granule exocytosis from cytokine trafficking. |
VAMP-8 KO mice, bone marrow-derived mast cell degranulation assays, confocal microscopy, SNARE complex immunoprecipitation, passive systemic anaphylaxis model |
Blood |
High |
18203950
|
| 2008 |
VAMP8 is the zymogen granule SNARE mediating basolateral exocytosis in alcoholic pancreatitis; ethanol exposure redirects apical to basolateral exocytosis in WT acini, but VAMP8-/- mice show blockade of both apical and basolateral exocytosis. Electron microscopy revealed reduced ZG-ZG homotypic fusions in VAMP8-/- acinar cells, establishing VAMP8 as critical for ZG-ZG fusion and basolateral secretion. |
VAMP8-/- mice, in vitro ethanol exposure + carbachol stimulation, amylase secretion assay, electron microscopy of ZG-ZG fusions |
The Journal of clinical investigation |
High |
18535671
|
| 2008 |
In mature human intestinal mast cells, VAMP-7 and VAMP-8 translocate to the plasma membrane and interact with SNAP-23 and STX-4 upon activation; inhibition of VAMP-7 or VAMP-8 (but not VAMP-2 or VAMP-3) markedly reduces IgE receptor-mediated histamine release, defining VAMP-7 and VAMP-8 as the required v-SNAREs for human mast cell degranulation. |
Primary human mast cell isolation, VAMP peptide inhibition, SNAP-23/STX-4 co-immunoprecipitation, histamine release assay |
European journal of immunology |
Medium |
18253931
|
| 2009 |
VAMP8 is localized to CTL lytic granules; VAMP8-/- CTL show normal immunological synapse formation and granule polarization but significantly reduced granzyme A and granzyme B secretion, establishing VAMP8 as a v-SNARE required for lytic granule fusion with the plasma membrane during CTL-mediated killing. |
VAMP8-/- mice, CTL cytotoxicity assay, granzyme secretion assay, immunofluorescence colocalization |
European journal of immunology |
High |
19830729
|
| 2009 |
VAMP8 localizes to secretory granules in macrophages and mediates TNF-alpha release; TNF-alpha co-localizes with VAMP8-positive vesicles in WT macrophages, while VAMP8-/- macrophages show inhibited TNF-alpha secretion and reduced degranulation. VAMP8-/- mice are protected from C5a-induced neutropenia, peritonitis, and systemic inflammation. |
VAMP8-/- mice, macrophage degranulation assay, TNF-alpha ELISA, confocal colocalization, in vivo peritonitis model |
Journal of immunology |
High |
19564343
|
| 2010 |
VAMP8 depletion in mice causes hydronephrosis and a 3–5-fold increase in aquaporin 2 (AQP2) levels; vasopressin/forskolin-induced AQP2 exocytosis is impaired in VAMP8-null collecting duct cells. VAMP8 co-localizes with AQP2 on intracellular vesicles and interacts with syntaxin 4 and syntaxin 3 t-SNAREs, establishing a role in regulated AQP2 trafficking to the plasma membrane. |
VAMP8-null mice, immunofluorescence colocalization, exocytosis assay in collecting duct cells, co-immunoprecipitation |
Molecular and cellular biology |
High |
19841070
|
| 2010 |
Knockdown of Vti1b and VAMP8 with siRNA disturbs autophagosome-lysosome fusion (LC3/LAMP1 colocalization reduced) without affecting bacterial invasion efficiency, but impairs cellular bactericidal efficiency in xenophagy (Group A Streptococcus). The same SNARE pair (VAMP8 + Vti1b) is required for canonical autophagosome-lysosome fusion; knockdown of syntaxin 7 or syntaxin 8 had little effect on autophagic fusion. |
siRNA knockdown, confocal microscopy for LC3/LAMP1 colocalization, bacterial survival assay, canonical autophagy LC3-II degradation assay |
Molecular biology of the cell |
High |
20089838
|
| 2010 |
In VAMP8-null mice, sarcolemmal GLUT4 levels are increased in both basal and insulin-stimulated states without change in total GLUT4, indicating VAMP8 is required for endocytosis of the insulin-responsive GLUT4 transporter. VAMP8-null mice display fasting hypoglycemia, enhanced glucose tolerance, and increased skeletal muscle glucose uptake. |
VAMP8-null mice, euglycemic-hyperinsulinemic clamp with radiotracer glucose uptake, immunofluorescence microscopy for sarcolemmal GLUT4 |
Diabetes |
High |
20876717
|
| 2010 |
Vti1b-deficient and Vamp8-deficient CTL show significantly reduced degranulation (CD107a surface exposure) and ~50% reduced cytotoxic activity after 3 days of antigen-specific stimulation; by day 4, cytotoxic activity is no longer impaired, suggesting a compensable role for both SNARE proteins in lytic granule exocytosis during early CTL development. |
Vti1b-KO and Vamp8-KO TCR-transgenic OT-I mice, CD107a degranulation assay, cytolytic activity assay |
Journal of immunology |
Medium |
20543108
|
| 2011 |
VAMP8 is specifically required for sequential (granule-to-granule) compound exocytosis in pancreatic acinar cells. Using an assay distinguishing primary (granule-plasma membrane) from secondary (granule-granule) fusion events, VAMP8-KO acinar cells show specific reduction in secondary granule fusion but not primary fusion. Immunoprecipitation shows syntaxin 3 associates with VAMP8 for granule-granule fusion, while syntaxin 2 associates with VAMP2 for primary fusion. |
VAMP8-KO mice, two-photon live-cell imaging distinguishing primary vs. secondary fusion events, immunoprecipitation |
The Journal of biological chemistry |
High |
21733851
|
| 2011 |
VAMP8 localizes predominantly to goblet cell mucin granules in human airway epithelium; siRNA/shRNA knockdown of VAMP8 reduces mucin secretion stimulated by PAR agonists, neutrophil elastase, and ATP, as well as basal secretion. VAMP8-KO mice with IL-13-induced mucous metaplasia show reduced mucin in bronchoalveolar lavage. Knockdown of VAMP2 or VAMP3 does not affect mucin secretion. |
VAMP8 siRNA/shRNA knockdown in airway epithelial cell cultures, mucin secretion assay, VAMP8-KO mice with mucous metaplasia model, immunolocalization |
The Journal of physiology |
High |
22144578
|
| 2012 |
VAMP8-null mice show impaired insulin granule recruitment to the plasma membrane contributing to reduced GLP-1 potentiation of glucose-stimulated insulin secretion; however, VAMP8-null mice also display increased islet β cell mass from enhanced β cell mitosis, amplified by GLP-1, demonstrating a dual role of VAMP8 in insulin granule exocytosis and islet β cell growth. |
VAMP8-null mice, glucose-stimulated insulin secretion assay, islet morphometry, β cell proliferation assay, GLP-1 treatment |
Cell metabolism |
High |
22841572
|
| 2013 |
The Leishmania surface metalloprotease GP63 cleaves VAMP8 (among other SNAREs) on phagosomes. GP63-mediated VAMP8 inactivation (or Vamp8 gene disruption) prevents NADPH oxidase (NOX2) complex assembly on phagosomes, altering phagosomal pH and degradative properties, and inhibiting MHC class I cross-presentation of Leishmania antigens, thereby reducing T cell activation. |
GP63 cleavage of VAMP8 (biochemical), Vamp8 KO cells/mice, phagosomal NOX2 assembly assay, phagosomal pH measurement, MHC class I cross-presentation assay, T cell activation assay |
Cell host & microbe |
High |
23870310
|
| 2015 |
In primary human CTLs, VAMP8 co-localizes with Rab11a-positive recycling endosomes (not cytotoxic granules). Upon stimulation, VAMP8-positive recycling endosomes traffic to and fuse with the plasma membrane at immune synapses before cytotoxic granule fusion. VAMP8 knockdown blocks both recycling endosome and cytotoxic granule fusion. Mechanistically, VAMP8-dependent recycling endosome fusion deposits syntaxin-11 at immune synapses to facilitate assembly of plasma membrane SNARE complexes required for cytotoxic granule exocytosis. |
Confocal and TIRF microscopy in primary human CTLs, VAMP8 siRNA knockdown, live-cell imaging of vesicle fusion kinetics, syntaxin-11 localization assay |
The Journal of cell biology |
High |
26124288
|
| 2015 |
Starvation induces Sbf/MTMR13 GEF activity and RAB21 activation, which promotes MTMR13 and RAB21 binding to VAMP8, facilitating endolysosomal trafficking of VAMP8 to lysosomes required for autophagosome-lysosome fusion. Depletion of Sbf/MTMR13 or Rab21 blocks VAMP8 endolysosomal delivery and impairs starvation-induced autophagy. |
Drosophila and mammalian cell depletion experiments, Rab21 GEF activity assay, co-immunoprecipitation of MTMR13/RAB21 with VAMP8, autophagy flux assay, endolysosomal trafficking assay |
EMBO reports |
Medium |
25648148
|
| 2017 |
VAMP8 mediates NOX2 trafficking not only to phagosomes but also to endosomes in both human and mouse dendritic cells. Absence of VAMP8 leads to decreased ROS production, reduced lipid peroxidation, impaired antigen translocation to cytosol, and impaired cross-presentation; VAMP8 knockdown did not affect MHC class I or TAP1 recruitment to phagosomes. |
VAMP8 knockdown in human and mouse DCs, NOX2 recruitment assay, ROS measurement, lipid peroxidation assay, antigen translocation and cross-presentation assay |
European journal of cell biology |
Medium |
28688576
|
| 2017 |
APOL1 protein interacts with VAMP8 in podocytes; this interaction was confirmed by co-immunoprecipitation and surface plasmon resonance. APOL1 disease-associated variants attenuate this interaction. Molecular dynamics simulations and circular dichroism spectroscopy reveal that variant APOL1 has increased C-terminal conformational stability (a more closed/autoinhibited state), reducing interaction with VAMP8-coated vesicles. |
Co-immunoprecipitation, surface plasmon resonance, molecular dynamics simulation, circular dichroism spectroscopy, structural homology search |
JCI insight |
Medium |
28724794
|
| 2017 |
VAMP8 is present on mucin granules in intestinal goblet cells and is specifically activated during Entamoeba histolytica infection to coordinate mucin exocytosis; ablation of VAMP8 impairs mucin secretion, increases E. histolytica adherence and epithelial cell apoptosis, and triggers a proinflammatory response (IL-1α, IL-1β, TNF-α). |
VAMP8 siRNA knockdown in human goblet cells, Vamp8-/- mice, E. histolytica infection model, mucin secretion assay, apoptosis assay, cytokine measurement |
mBio |
High |
28974617
|
| 2017 |
VAMP8 knockdown reduced JAK1 and STAT1 phosphorylation and impaired induction of interferon-stimulated genes (ISGs) following West Nile virus infection or IFN-β treatment; VAMP8-mediated STAT1 phosphorylation required presence of TRIM6, identifying VAMP8 as a novel regulator of type I interferon signaling downstream of TRIM6. |
VAMP8 siRNA knockdown in human cells, phospho-JAK1/STAT1 western blotting, ISG induction assay, next-generation sequencing identification of VAMP8 |
Journal of virology |
Medium |
31694946
|
| 2018 |
VAMP8 interacts with the metastasis suppressor GTPase RAB37; confocal and TIRF microscopy show VAMP8 co-localizes with RAB37 and facilitates trafficking of RAB37-TIMP1 vesicles. VAMP8 is required for RAB37-regulated exocytosis of TIMP1 to suppress lung cancer metastasis, demonstrated by tail-vein injection reconstitution experiments. |
Co-immunoprecipitation, confocal and TIRF microscopy, exocytosis/secretion assay for TIMP1, tail-vein injection metastasis model, lung-to-lung metastasis reconstitution |
Cancer letters |
Medium |
30165196
|
| 2019 |
VAMP8 coordinates MUC2 mucin exocytosis from colonic goblet cells; Vamp8-/- mice exhibit altered mucus layer, increased encounters with microbial antigens, shift to detrimental microbiota, mild basal pro-inflammatory state, and high susceptibility to chemical and infectious colitis, demonstrating essential role of VAMP8 in intestinal homeostasis via mucus exocytosis. |
Vamp8-/- mice, mucin secretion assay, intestinal microbiota analysis, colitis models (chemical and infectious), immunology assays |
Nature communications |
High |
31541089
|
| 2019 |
Defective AP-3-dependent trafficking in Hermansky-Pudlak Syndrome type 2 (HPS2) endothelial cells depletes VAMP8 from Weibel-Palade bodies; CRISPR-Cas9-engineered VAMP8-/- endothelial cells show impaired stimulus-induced von Willebrand factor secretion, establishing VAMP8 as an AP-3-dependent SNARE required for Weibel-Palade body exocytosis. |
Patient-derived blood outgrowth endothelial cells, CRISPR-Cas9 KO of VAMP8, proteome analysis, von Willebrand factor secretion assay |
Haematologica |
High |
30630984
|
| 2021 |
mTORC1 directly phosphorylates VAMP8, inhibiting formation of the STX17-SNAP29-VAMP8 SNARE complex and thereby blocking autophagosome-lysosome fusion. A VAMP8 phosphorylation mimic mutant fails to promote autophagosome-lysosome fusion in vitro. Dephosphorylated VAMP8 promotes recruitment of SCFD1 (Sec1/Munc18-like protein) to autolysosomes; phosphorylated VAMP8 or SCFD1 depletion inhibits fusion. Expression of phosphomimic VAMP8 in mouse liver increases lipid droplet accumulation. |
mTORC1 kinase assay (phosphorylation), in vitro fusion assay with phosphomimic VAMP8, SCFD1 localization assay, Co-IP for SNARE complex, liver lipid droplet assay |
Nature communications |
High |
34785650
|
| 2021 |
VAMP8 on lysosomes assists in forming prefusion clusters of multiple lysosomes around individual autophagosomes upon stimulation. A VAMP8 phosphorylation mimic reduces fusion in a lipid-mixing ensemble assay and increases unfused lysosomes associated with autophagosomes, suggesting phosphorylation minimizes spontaneous autophagosome-lysosome fusion under normal conditions while pre-assembling lysosomes for stimulated autophagy. |
Structured illumination microscopy, ensemble lipid-mixing fusion assay, VAMP8 phosphorylation mimic mutation |
Cell death & disease |
Medium |
34645799
|
| 2023 |
NRF2 transcriptionally maintains VAMP8 expression; NRF2-knockout cells have low VAMP8, which blocks autophagosome-lysosome fusion (ferritinophagy), leading to apoferritin accumulation in autophagosomes and an elevated labile iron pool, enhancing sensitivity to ferroptosis. |
NRF2 knockout cells, VAMP8 protein/mRNA measurement, LC3/LAMP1 colocalization assay, ferritin/NCOA4 immunoblotting, ferroptosis assay |
Science advances |
Medium |
36724221
|
| 2024 |
DRAM1 physically interacts with VAMP8 on lysosomes; this interaction is enhanced upon autophagy stimulation. DRAM1 preferentially promotes autophagosome-lysosome fusion by enhancing assembly of the STX17-SNAP29-VAMP8 complex. DRAM1 stabilizes lysosomal VAMP8 by inhibiting CHIP-mediated ubiquitination of VAMP8 at Lys68, 72, and 75, competitively binding CHIP. |
Co-immunoprecipitation, STX17-SNAP29-VAMP8 complex assembly assay, ubiquitination assay, CHIP-VAMP8 binding competition, site-directed mutagenesis of Lys68/72/75, autophagy flux assay |
Nature communications |
High |
40595569
|
| 2007 |
Salmonella SopB-generated PtdIns(3)P directly binds VAMP8/endobrevin and recruits it to Salmonella-induced macropinosomes in a nocodazole-dependent, Brefeldin A-independent manner; knockdown of VAMP8 or expression of truncated VAMP8 (1-79aa) reduces Salmonella invasion efficiency to the level of SopB phosphatase-dead mutant, demonstrating that bacteria exploit VAMP8 and PtdIns(3)P binding to promote phagocytosis. |
PtdIns(3)P–VAMP8 direct binding assay, VAMP8 siRNA knockdown, confocal colocalization, pharmacological inhibitors (wortmannin, nocodazole, Brefeldin A), bacterial invasion assay |
Traffic |
Medium |
17645435
|
| 2014 |
VAMP8-mediated ZG exocytosis depends on constitutive-like secretory pathway via early endosomal proteins Rab5/D52/EEA1; VAMP8-/- acini show >90% decrease in Rab5/D52/EEA1 and increased Rab11a/TI-VAMP7 on ZGs. GDP-trapped Rab11a-S25N specifically inhibits the VAMP8 but not VAMP2 secretion pathway; rescue of Rab5/D52/EEA1 expression restores VAMP8-dependent secretion. |
VAMP8-/- acini, Rab11a dominant-negative expression, adenoviral D52/Rab5 rescue, perifusion secretion kinetics assay, confocal colocalization |
The Journal of biological chemistry |
High |
25138214
|
| 2018 |
O-GlcNAc modification of SNAP29 inhibits formation of the SNAP29-STX17-VAMP8 SNARE complex; co-immunoprecipitation in diabetic rat cardiomyocytes showed that increased O-GlcNAc-SNAP29 disrupts STX17-VAMP8 complex assembly, blocking autophagic flux and exacerbating myocardial injury. |
Co-immunoprecipitation of SNAP29-STX17-VAMP8 complex, O-GlcNAc modification assay, STZ diabetic rat model, thiamet G and DON pharmacological tools, autophagy flux assay |
International journal of molecular medicine |
Medium |
30221662
|
| 2009 |
In dendritic cells, caspases regulate VAMP-8 expression; VAMP-8 protein is a substrate of caspases, and treatment with caspase inhibitor upregulates VAMP-8. Consistent with VAMP-8's role in inhibiting phagocytosis in DCs, immature DCs treated with caspase inhibitor show lower phagocytosis activity. |
Caspase inhibitor treatment, VAMP-8 expression analysis, phagocytosis assay, identification of caspase cleavage sites on VAMP-8 |
Biochemical and biophysical research communications |
Low |
19607812
|
| 2020 |
VAMP8 overexpression in neuronal cells (N2a) significantly increases tau secretion via late endosome-plasma membrane fusion, reducing intracellular tau levels; TIRF microscopy shows fusion of VAMP8-positive vesicles with plasma membrane correlates with cytoplasmic tau depletion. VAMP8 overexpression also reduces intracellular α-synuclein by increasing secretion. |
VAMP8 overexpression in N2a cells and murine hippocampal slices, intracellular/extracellular tau quantification, TIRF microscopy of VAMP8-positive vesicle fusion |
The Journal of biological chemistry |
Medium |
33454017
|
| 2022 |
Oxidative stress inhibits endocytosis, decreasing lysosomal localization of VAMP8 and blocking autophagosome-lysosome fusion in human neuroblastoma cells; treatment with an endocytosis inhibitor recapitulates the VAMP8 lysosomal depletion and autophagy block, establishing that endocytic trafficking is required for VAMP8 delivery to lysosomes for autophagy. |
Oxidative stress induction, endocytosis inhibitor treatment, lysosomal VAMP8 localization assay (immunofluorescence), autophagosome-lysosome fusion assay |
Biological & pharmaceutical bulletin |
Low |
36328496
|
| 2023 |
CENPN inhibits VAMP8 transcription by reducing phospho-CREB binding to the VAMP8 promoter; CENPN knockdown increases p-CREB nuclear translocation and VAMP8 expression, enhancing autophagic flux and paclitaxel sensitivity in nasopharyngeal carcinoma. Sequential knockdown of CENPN and VAMP8 reverses the PTX-sensitizing effect of CENPN knockdown, confirming VAMP8 as the mediator. |
ChIP assay for p-CREB binding to VAMP8 promoter, siRNA/shRNA knockdown, autophagy flux assay, nude mouse xenograft PTX sensitivity assay |
Autophagy |
Medium |
37776538
|
| 2023 |
VAMP8 interacts with DDX5 in osteosarcoma cells; this interaction promotes DDX5 degradation via the ubiquitin-proteasome system, reducing β-catenin levels and suppressing EMT and metastasis. VAMP8 also promotes autophagy flux as a potential additional metastasis-suppressive mechanism. |
Co-immunoprecipitation of VAMP8-DDX5, ubiquitin-proteasome inhibitor experiments, β-catenin expression, EMT marker analysis, invasion/migration assays |
Cancer biology & therapy |
Low |
37405957
|