| 1999 |
VAMP7 localizes to late endosomes and lysosomes (co-localizing with LAMP-1) and antibodies against its cytoplasmic domain inhibit EGF receptor degradation (endosome-to-lysosome transport) but not transferrin recycling in streptolysin-O-permeabilized cells, establishing a role in vesicular transport from endosomes to lysosomes. |
Monoclonal/polyclonal antibody generation, immunohistochemistry, immunoelectron microscopy, streptolysin-O permeabilized cell transport assay |
The Journal of cell biology |
High |
10459012
|
| 1999 |
In neurons, VAMP7/TI-VAMP localizes to a novel membrane compartment distinct from synaptic vesicles and large dense-core granules, concentrating in the leading edge of growth cones before synaptogenesis, suggesting a specialized exocytic vesicle pool for neurite outgrowth. |
Subcellular fractionation, immunoelectron microscopy, immunofluorescence in hippocampal neurons and PC12 cells |
The Journal of neuroscience |
Medium |
10559389
|
| 2000 |
VAMP7 is required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophages; a soluble dominant-negative VAMP7 fragment (lacking transmembrane domain) inhibited both heterotypic late endosome-lysosome fusion and homotypic lysosome fusion in an in vitro cell-free fusion assay. |
In vitro cell-free fusion assay with dominant-negative bacterially-expressed VAMP7 fragment |
Molecular biology of the cell |
High |
10888671
|
| 2000 |
VAMP7/TI-VAMP is essential for vesicular transport mediating neurite outgrowth in staurosporine-differentiated PC12 cells; the N-terminal Longin domain inhibits association with SNAP-25, and expression of this domain blocks neurite outgrowth as potently as Botulinum neurotoxin E (which cleaves SNAP-25), while deletion of the Longin domain increases SNARE complex formation and strongly stimulates neurite outgrowth. |
Dominant-negative N-terminal domain expression, co-immunoprecipitation of SNARE complexes, neurite outgrowth assay in PC12 cells |
The Journal of cell biology |
High |
10811829
|
| 2000 |
In RBL-2H3 mast cells, VAMP7 localizes exclusively in granule membranes (not plasma membrane); upon antigen stimulation, VAMP7-positive granules move to the cell surface via fusion with the plasma membrane, suggesting VAMP7 mediates degranulation. |
RT-PCR, GFP-fusion protein live imaging, confocal microscopy |
Biochemical and biophysical research communications |
Medium |
10777677
|
| 2001 |
Syntaxin 7 forms SNARE complexes with either VAMP7 or VAMP8 (together with Syntaxin 6 and mVti1b) in B16 melanoma cells, as identified by large-scale Syntaxin 7 immunoprecipitation followed by mass spectrometry, indicating combinatorial SNARE assembly in the late endosomal pathway. |
Immunoaffinity purification, electrospray mass spectrometry, immunoblotting, immunofluorescence colocalization |
The Journal of biological chemistry |
Medium |
11278762
|
| 2002 |
In Dictyostelium discoideum, VAMP7 forms an active SNARE complex with Syntaxin 7, Vti1 and Syntaxin 8 in endosomes; co-immunoprecipitation and MS identified these partners, and soluble recombinant VAMP7 fragment inhibited in vitro reconstituted endosome fusion. |
Co-immunoprecipitation, mass spectrometry peptide sequencing, in vitro endosome fusion assay with recombinant VAMP7 fragment |
The Biochemical journal |
High |
12175335
|
| 2003 |
Ectopic expression of the plasma membrane t-SNARE syntaxin 1 in the ER redirects TI-VAMP/VAMP7 (and cellubrevin) to the ER in a microtubule-dependent manner, and TI-VAMP associates in vivo with exogenous syntaxin 1, demonstrating that the destination of v-SNAREs is driven by specific interactions with cognate t-SNAREs. |
Ectopic expression, co-immunoprecipitation, immunofluorescence, microtubule depolymerization |
Journal of cell science |
Medium |
12759369
|
| 2004 |
The Q-SNAREs syntaxin 7, Vti1b, and syntaxin 8 can pair with either VAMP8 (for homotypic late endosome fusion) or VAMP7 (for heterotypic late endosome–lysosome fusion), as shown by antibody inhibition in rat liver cell-free fusion systems and separate co-immunoprecipitation of syntaxin 7 complexes with VAMP7 or VAMP8. Overexpression of the VAMP7 N-terminal domain in fibroblasts inhibited mixing of lysosomal and late endosomal content markers. |
Antibody inhibition in rat liver cell-free fusion assay, co-immunoprecipitation, dominant-negative N-terminal domain overexpression, content-mixing assay |
EMBO reports |
High |
15133481
|
| 2004 |
TI-VAMP/VAMP7 mediates late endocytic compartment exocytosis required for optimal Fc receptor- and complement receptor-mediated phagocytosis in macrophages; dominant-negative Longin domain expression and siRNA depletion of TI-VAMP blocked pseudopod extension and phagosome sealing. |
Dominant-negative domain expression, siRNA knockdown, scanning electron microscopy, exocytosis assays in macrophages |
The EMBO journal |
High |
15470500
|
| 2004 |
Hypertonicity-stimulated GLUT4 recruitment to the muscle cell surface is dependent on TI-VAMP/VAMP7 (but not VAMP2), as shown by siRNA knockdown of TI-VAMP reducing basal and hypertonicity-stimulated surface GLUT4; insulin stimulation was only partly reduced, indicating TI-VAMP and VAMP2 mediate GLUT4 trafficking from distinct pools. |
siRNA knockdown, surface GLUT4myc quantification, dominant-negative NSF expression in L6 myoblasts |
Molecular biology of the cell |
Medium |
15469990
|
| 2005 |
Cdc42 and F-actin control the polarized accumulation and exocytosis of TI-VAMP/VAMP7-containing vesicles in hippocampal neuron growth cones; dominant-positive Cdc42 stimulates TI-VAMP exocytosis in an actin-dependent manner, as measured by pHLuorin-tagged TI-VAMP fluorescence. |
Dominant-positive Cdc42 expression, pHLuorin exocytosis assay, actin disruption, immunofluorescence in hippocampal neurons |
Molecular biology of the cell |
Medium |
16381811
|
| 2006 |
TI-VAMP/VAMP7 is insensitive to botulinum neurotoxin B due to at least 12 amino acid differences from VAMP-2 scattered along a 22-residue interface; replacement of specific residues (including Ile158, Thr161, and section 165-174) with VAMP-2 equivalents progressively restored cleavability. |
In vitro cleavage assays with chimeric VAMP7/VAMP2 hybrid proteins and point mutants |
Journal of molecular biology |
High |
16430921
|
| 2007 |
The Longin domain of TI-VAMP/VAMP7 has dual biochemical functions: it inhibits SNARE complex formation and binds to the δ subunit of AP-3, targeting TI-VAMP to late endosomes. Expression of the isolated Longin domain disrupts AP-3δ localization, impairs lysosomal secretion, blocks membrane repair after wounding, and inhibits epithelial cell migration. |
Inducible Longin domain expression in MDCK cells, immunofluorescence, lysosomal secretion assay, wound healing assay, electron microscopy |
Biology of the cell |
Medium |
17288539
|
| 2007 |
VAMP7 is required for granzyme B release and target cell killing in NK cell line YT-Indy; siRNA knockdown of VAMP7 reduced granzyme B secretion to <1 ng/mL compared to 1.5-2.5 μg/mL in controls and caused a 7-fold reduction in NK cell-mediated Jurkat killing. |
siRNA knockdown, granzyme B secretion assay, cytotoxicity assay |
Biochemical and biophysical research communications |
Medium |
18042464
|
| 2008 |
Clathrin-mediated endocytosis of VAMP7 is directly mediated by the ArfGAP/clathrin adaptor Hrb, which wraps 20 residues of its unstructured C-terminal tail around the VAMP7 longin domain; disrupting this interaction causes VAMP7 accumulation at the cell surface. The VAMP7 SNARE helix can fold back onto the longin domain to compete with Hrb, suggesting Hrb-mediated endocytosis occurs preferentially when VAMP7 is in a cis-SNARE complex. |
Crystal structure of Hrb-VAMP7 longin domain complex, site-directed mutagenesis, Hrb depletion, cell surface VAMP7 quantification |
Cell |
High |
18775314
|
| 2008 |
VAMP7 and VAMP8 are required for activation-induced degranulation in primary human mast cells; both SNAREs translocate to the plasma membrane and interact with SNAP-23 and STX-4 upon activation, whereas VAMP2 and VAMP3 knockdown did not inhibit IgE receptor-mediated histamine release. |
SNARE inhibition (specific approaches), co-immunoprecipitation, histamine release assay, translocation assay in primary human intestinal mast cells |
European journal of immunology |
Medium |
18253931
|
| 2009 |
VAMP3 mediates fusion of MVBs with autophagosomes to form amphisomes, whereas VAMP7 mediates the subsequent fusion of amphisomes/autophagosomes with lysosomes to complete autophagy. VAMP7 and NSF also participate in MVB fusion with the plasma membrane to release exosomes. |
siRNA knockdown of VAMP3 or VAMP7 in K562 cells, morphological and biochemical autophagy assays, exosome secretion assay |
Biochimica et biophysica acta |
Medium |
19781582
|
| 2009 |
TI-VAMP/VAMP7 interacts with Varp (a Rab21 GEF) through a specific interacting domain (ID); Varp, TI-VAMP, and Rab21 co-localize in the perinuclear region and in transport vesicles of differentiating hippocampal neurons. Silencing Varp or expressing the ID or GEF-dead Varp impairs neurite growth, while a GTP-hydrolysis-defective Rab21 mutant enhances it. |
Co-immunoprecipitation, siRNA knockdown, dominant-negative expression, neurite growth assay, colocalization in hippocampal neurons |
EMBO reports |
Medium |
19745841
|
| 2009 |
A SNARE complex containing VAMP7 and Vti1a defines a novel non-conventional trafficking pathway to the cell surface used by KChIP1 and Kv4 potassium channels; siRNA knockdown of Vti1a or VAMP7 inhibited Kv4/KChIP1 surface delivery without affecting VSVG conventional trafficking. |
siRNA knockdown, surface delivery assay, colocalization, comparison with VSVG conventional trafficking |
The Biochemical journal |
Medium |
19138172
|
| 2010 |
VAMP7/TI-VAMP adopts a preferentially closed conformation in solution, where the SNARE helix folds back onto the longin domain, as established by NMR backbone resonance assignments, chemical shift perturbation analysis, and hydrogen/deuterium exchange experiments. |
NMR spectroscopy (backbone resonance assignment, chemical shift perturbation, H/D exchange) |
The Journal of biological chemistry |
High |
20378544
|
| 2010 |
TI-VAMP/VAMP7 depletion enhances clathrin-dependent endocytosis of activated EGFR by reducing cell-surface CD82 (a tetraspanin that controls EGFR microdomain localization); TI-VAMP-positive vesicles transport CD82 from the Golgi to the cell surface, and its loss restrains EGFR diffusion and impairs MAPK signaling. |
siRNA depletion, quantum dot single-particle tracking, co-immunoprecipitation, Golgi-to-surface secretion assay |
Journal of cell science |
Medium |
20144992
|
| 2011 |
VAMP7 controls exocytosis of proteolipid protein (PLP) from late endosomal/lysosomal organelles as part of a transcytosis pathway in oligodendrocytes; siRNA silencing and dominant-negative expression reduced PLP at the cell surface and at myelin-like membranes in co-culture with neurons. AP-3δ-deficient mocha mice with VAMP7 missorting show mild dysmyelination with reduced PLP levels. |
siRNA knockdown, dominant-negative expression, co-culture with cortical neurons, AP-3δ-deficient mouse model analysis |
The Journal of neuroscience |
Medium |
21490207
|
| 2011 |
VAMP4 and VAMP7 both colocalize with lytic granules in NK cells during cytotoxic interactions; only VAMP7 associates with perforin-containing granules in resting cells. Disruption of either VAMP4 or VAMP7 inhibits lytic granule exocytosis and NK cytotoxic activity, but only VAMP7 is required for IFN-γ secretion. |
siRNA knockdown in YTS and primary NK cells, cytotoxicity assay, granule exocytosis assay, IFN-γ secretion assay, colocalization |
European journal of immunology |
Medium |
21805468
|
| 2011 |
VAMP7 knockout mice show reduced neurite outgrowth in cultured hippocampal neurons, but lysosomal exocytosis was not affected in mutant fibroblasts, and apical protein localization in kidney/intestine was normal, demonstrating a selective role in neuronal axon extension. |
VAMP7 knockout mouse generation, neurite outgrowth assay, lysosomal exocytosis assay, immunohistochemistry in vivo |
Traffic |
High |
21740490
|
| 2012 |
Varp binds directly to VAMP7, trapping its SNARE motif between Varp's second ankyrin repeat domain and the VAMP7 longin domain, thereby kinetically inhibiting VAMP7 SNARE complex formation; this inhibition is increased when Varp simultaneously binds Rab32-GTP on the same membrane. |
Crystal structure of Varp ankyrin repeat domain 2 in complex with VAMP7 cytosolic portion, co-immunoprecipitation, SNARE complex formation assay |
Nature structural & molecular biology |
High |
23104059
|
| 2012 |
Varp interacts with GolginA4 and kinesin 1 (Kif5A), and activated Rab21-GTP binds MACF1, an actin/microtubule regulator that is itself a GolginA4 partner; these components are collectively required for directed anterograde movement of TI-VAMP/VAMP7 vesicles from the cell center to the periphery. |
Co-immunoprecipitation, siRNA knockdown, live-cell imaging of VAMP7 vesicle dynamics |
Developmental cell |
Medium |
22705394
|
| 2012 |
TI-VAMP/VAMP7 is the vesicular SNARE that mediates secretory lysosome exocytosis in astrocytes, contributing to ATP and cathepsin B release; downregulation of TI-VAMP inhibited ATP-storing vesicle fusion, ATP-mediated calcium wave propagation, and cathepsin B secretion from glioma cells. |
siRNA knockdown, live-cell Ca2+ imaging, ATP secretion assay, cathepsin B secretion assay |
Biology of the cell |
Medium |
22188132
|
| 2012 |
VAMP7 mediates ATP release from autophagic vesicles to the extracellular space; upon starvation, VAMP7-positive/LC3-positive vesicles redistribute to the cell periphery in a microtubule-, KIF5-, and RAB7/RILP-dependent manner and fuse with the plasma membrane to release ATP. |
siRNA knockdown, colocalization, ATP secretion assay, microtubule depolymerization, live-cell imaging |
Autophagy |
Medium |
22951367
|
| 2012 |
VAMP7 knockout mice show increased anxiety behavior and decreased brain weight, with increased third ventricle volume; axon growth appeared normal in knockout cultured neurons, suggesting compensatory mechanisms and an unexpected role of TI-VAMP-mediated vesicular traffic in anxiety. |
Constitutive VAMP7 knockout mouse (exon 3 deletion), behavioral characterization, neuroanatomical analysis, cultured neuron axon growth assay |
The Journal of neuroscience |
Medium |
22323709
|
| 2012 |
The AP-3 δ-adaptin subunit linker binds the VAMP7 longin domain; the crystal structure shows the interaction requires VAMP7 SNARE motif engagement in a SNARE complex. Mutation of binding residues on either partner abolishes interaction in vitro and in vivo, and abolishes VAMP7 rescue of its mislocalization in mocha (δ-adaptin-null) fibroblasts. |
Crystal structure of δ-adaptin linker–VAMP7 longin domain complex, site-directed mutagenesis, in vivo mislocalization rescue assay in mocha fibroblasts |
Developmental cell |
High |
22521722
|
| 2013 |
VAMP7 is required for the recruitment and phosphorylation of Lat-containing vesicles to TCR-activation sites during T cell activation; VAMP7 silencing (by siRNA and in VAMP7-knockout mice) blocked Lat vesicle recruitment without requiring vesicle–plasma membrane fusion, impaired Lat phosphorylation, TCR-Lat signaling complex formation, and T cell activation. |
siRNA silencing, VAMP7-knockout mice, live-cell imaging, phospho-Lat biochemistry, T cell activation assays |
Nature immunology |
High |
23666293
|
| 2013 |
Reelin selectively enhances spontaneous (but not evoked) neurotransmitter release via a presynaptic mechanism requiring VAMP7 and SNAP-25 but not synaptobrevin2, VAMP4, or vti1a; the effect requires a modest ApoER2-dependent increase in presynaptic Ca2+. |
Genetic perturbation (VAMP7 knockout, shRNA knockdown of specific SNAREs), electrophysiology, presynaptic Ca2+ imaging |
Neuron |
High |
24210904
|
| 2013 |
hVps41 and VAMP7 function in a parallel, direct TGN-to-late endosome transport pathway for LAMP-1 and LAMP-2, distinct from clathrin/M6PR-dependent lysosomal enzyme trafficking; knockdown of hVps41 or VAMP7 caused accumulation of LAMP carriers, while knockdown of hVps39 or hVps18 did not, indicating hVps41 acts independently of CORVET/HOPS. |
siRNA knockdown, immunoelectron microscopy of endogenous LAMP carriers, LAMP-1-mGFP trafficking assay |
Nature communications |
High |
23322049
|
| 2013 |
TI-VAMP/VAMP7 exocytosis is activated by c-Src kinase-mediated phosphorylation of tyrosine 45 in the Longin domain; a Y45E phosphomimetic mutant activates both t-SNARE binding and exocytosis, whereas Y45F does not, establishing phosphorylation as a molecular switch relieving Longin domain autoinhibition. |
In vitro kinase assay with c-Src, site-directed mutagenesis (Y45E and Y45F), SNARE complex formation assay, exocytosis assay |
The Journal of biological chemistry |
High |
23471971
|
| 2014 |
VAMP7 co-localizes with estrogen receptor α (ESR1) in the presence of 17β-estradiol; elevated VAMP7 levels intensify ESR1-potentiated transcriptional activity by increasing ESR1 protein cellular content upon ligand stimulation, upregulating estrogen-responsive genes (ATF3, CYR61, CTGF) and causing urogenital development defects. |
Transgenic mouse (human VAMP7 BAC), co-localization experiments, transcriptional reporter assays, gene expression analysis |
Nature medicine |
Medium |
24880616
|
| 2014 |
SNAP23, Syntaxin4, and VAMP7 form a SNARE complex at invadopodia during tumor cell invasion; coimmunoprecipitation showed increased SNAP23-Syntaxin4-VAMP7 association during invadopodium formation, which correlated with decreased Syntaxin4 phosphorylation. Blocking these SNAREs perturbed MT1-MMP delivery, ECM degradation, and cell invasion. |
Co-immunoprecipitation, SNARE function blockade, invadopodium ECM degradation assay, invasion assay |
Molecular biology of the cell |
Medium |
24807903
|
| 2015 |
VAMP7-deficient platelets show partial defects in dense granule and α-granule exocytosis and impaired spreading on matrices; VAMP7 co-immunoprecipitates with VARP and Arp2/3, and these proteins colocalize at the platelet periphery during spreading, suggesting VAMP7 links granule exocytosis with actin reorganization via the VARP–Arp2/3 axis. |
VAMP7-knockout mouse platelets, granule exocytosis assay, aggregation assay, spreading assay, co-immunoprecipitation of VAMP7–VARP–Arp2/3 |
Blood |
High |
25999457
|
| 2015 |
Apical exocytosis of NHE3, CFTR, and GLUT5 in polarized epithelial cells requires a cascade involving Rab11, Myo5B, Slp4a, Munc18-2, and Vamp7 with Stx3; CRISPR/genome-edited Myo5B mutation disrupts this pathway selectively, while brush border enzymes localize normally. |
CRISPR/genome editing of Myo5B in human epithelial cells, cargo-selective exocytosis assay, colocalization and interaction studies |
The Journal of cell biology |
Medium |
26553929
|
| 2015 |
VAMP7-positive lysosome-like vesicles interact with the Salmonella-containing vacuole (SCV) to promote Salmonella-induced filament formation and bacterial growth within the late SCV, as identified by quantitative proteomics of the SCV at defined time points post-invasion. |
Quantitative proteomics of isolated SCVs, functional follow-up with VAMP7-positive vesicle interaction assay |
Cellular microbiology |
Low |
26084942
|
| 2016 |
VAMP7 mediates constitutive transport of TRPM8 channel to the plasma membrane via atypical LAMP1-positive, non-acidic vesicles; VAMP7-deficient mice exhibit reduced TRPM8 functional expression in sensory neurons and concomitant deficits in cold avoidance and icilin-induced cold hypersensitivity. |
VAMP7-knockout mouse, live-cell imaging of TRPM8 vesicles, patch-clamp electrophysiology, cold avoidance behavioral assay |
Nature communications |
High |
26843440
|
| 2016 |
VAMP7 regulates autophagy to maintain mitochondrial homeostasis and control glucose-stimulated insulin secretion in pancreatic β-cells; β-cell-specific VAMP7 KO mice show defective autophagosome formation, accumulation of p62 on mitochondria, reduced ATP production, and impaired insulin secretion, which worsens on high-fat diet. |
β-cell-specific VAMP7 knockout mouse (Vamp7flox/Y;Cre), autophagy flux assay, mitochondrial function assay, glucose-stimulated insulin secretion |
Diabetes |
High |
26953164
|
| 2016 |
VAMP7-null dendritic cells show impaired multidirectional IL-12 secretion and complete failure of directed IL-12 release at the immune synapse; IL-12 localizes in VAMP7-positive late endocytic vesicles, and VAMP7-mediated release at the immune synapse drives T cell effector function acquisition. |
VAMP7-knockout mouse DCs, IL-12 secretion assay (ELISA), live-cell imaging of IL-12 vesicles at immune synapse, T cell activation assay |
Cell reports |
High |
26972013
|
| 2016 |
BLOC-1 regulates formation of tubular transport carriers delivering VAMP7 and TYRP1 cargo to melanosomes, while BLOC-3 (via its exchange factor activity toward RAB38) is required for formation of distinct VAMP7 recycling carriers from melanosomes that also contain VARP; these two pathways explain distinct hypopigmentation phenotypes in BLOC-1 and BLOC-3 deficiency. |
Live-cell imaging, siRNA knockdown of BLOC-1 and BLOC-3 components, colocalization, VAMP7 trafficking assay in melanocytes |
The Journal of cell biology |
Medium |
27482051
|
| 2017 |
Vamp7 is associated with Lamp-1+ lysosomal vesicles at the B-cell immune synapse; Vamp7 knockdown impairs local lysosomal secretion at the synapse without affecting lysosome transport to the interface, resulting in defective antigen extraction, processing, and MHC-II presentation. |
siRNA knockdown, live-cell imaging, lysosome secretion assay at immune synapse, antigen presentation assay |
Molecular biology of the cell |
Medium |
28179460
|
| 2017 |
Spastin KO in cortical neurons enhances the anterograde velocity of VAMP7-containing vesicles (but not VAMP2 vesicles) via increased acetylated tubulin levels that enhance kinesin-1 motor activity; pharmacological tubulin hyperacetylation recapitulates the VAMP7 axonal dynamics phenotype. |
SPG4 (spastin) KO neurons, live-cell imaging of VAMP7 and VAMP2 vesicles, tubulin acetylation analysis, pharmacological tubulin stabilization |
Biochimica et biophysica acta. Molecular basis of disease |
Medium |
28392418
|
| 2018 |
VAMP7 forms a ciliary targeting complex with Rab11 and Rab8 (binding to the VAMP7 longin domain), Rabin8 (interacting with the SNARE domain), and FIP3 (regulating VAMP7 access to Rab11); at the ciliary base, VAMP7 forms a complex with syntaxin 3 and SNAP-25, and the R-SNARE motif of VAMP7 is critical for intracellular trafficking. |
Co-immunoprecipitation of VAMP7 with Rab11/Rab8/Rabin8/FIP3, transgenic animal expression of VAMP7 mutants (ΔGFP-VAMP7, Y45E, R150E), colocalization with ciliary cargo rhodopsin |
Journal of cell science |
Medium |
30404838
|
| 2018 |
VAMP7 in pancreatic β-cells localizes in Atg9a-resident vesicles at recycling endosomes and interacts with Hrb, Syntaxin16, and SNAP-47; Hrb recruits VAMP7 and Atg9a from plasma membrane to recycling endosomes, while Syntaxin16/SNAP-47 mediate autophagosome formation, forming a SNARE complex required for autophagy. |
VAMP7-deficient β-cells, Min6 cell siRNA knockdown, co-immunoprecipitation, colocalization, autophagy assay |
Endocrinology |
Medium |
30215699
|
| 2018 |
LRRK1 binds the VAMP7 Longin domain and negatively regulates VAMP7-mediated lysosomal secretion; VARP positively controls the peripheral pool of secretory lysosomes; LRRK1 and VARP compete for VAMP7 binding. VAMP7-deficient cells are impaired in adaptation to substrate rigidity, and more rigid substrates stimulate VAMP7-mediated secretion in a Longin domain-dependent manner. |
Atomic force microscopy, co-immunoprecipitation of VAMP7-LRRK1 and VAMP7-VARP, VAMP7 KO cells, secretion assays on substrates of different rigidity |
iScience |
Medium |
30240735
|
| 2019 |
VAMP7 forms a SNARE complex with Syntaxin11 and SNAP-23 at the plasma membrane of human cytotoxic T lymphocytes and co-localizes with granule markers throughout T cell maturation; VAMP7 knockdown significantly reduces CTL killing efficiency without impairing early TCR signaling. |
siRNA knockdown, co-immunoprecipitation, live-cell imaging, cytotoxicity assay in primary human T cells |
Frontiers in immunology |
Medium |
31447853
|
| 2019 |
DIPK2A, a late endosome/lysosome-localized protein, binds VAMP7B (a SNARE-domain-disrupted isoform of VAMP7), relieving the competitive inhibition VAMP7B exerts on STX17 binding to functional VAMP7A, thereby enhancing autophagosome-lysosome fusion and autophagic degradation. |
Co-immunoprecipitation, siRNA knockdown, autophagy flux assay, apoptosis assay |
Autophagy |
Medium |
31251111
|
| 2020 |
VAMP7-dependent secretion of Reticulon 3 (RTN3) regulates neurite growth; VAMP7 KO neuronal secretomes contain less RTN3, expression of the inhibitory VAMP7 Longin domain disrupts RTN3 subcellular localization in neurons, and a nanobody against VAMP7 inhibits axonal overgrowth induced by nutrient restriction, connecting autophagy-related secretion to neurite growth. |
VAMP7 KO secretome mass spectrometry, Longin domain expression, anti-VAMP7 nanobody, conditioned medium experiments, ATG5 KO |
Cell reports |
Medium |
33357422
|
| 2023 |
Celastrol directly binds VAMP7 (and RAB7) as confirmed by Surface Plasmon Resonance; overexpression of VAMP7 blocks celastrol's inhibitory effects on autophagosome-lysosome fusion and apoptosis induction in preadipocytes. |
Surface Plasmon Resonance, overexpression rescue, autophagy flux assay, apoptosis assay |
Frontiers in pharmacology |
Medium |
36959859
|
| 2023 |
VAMP7j (a human-specific splice isoform lacking the SNARE motif but retaining longin and transmembrane domains) modulates neurite outgrowth in SH-SY5Y cells by mediating L1CAM transport to the plasma membrane in a manner regulated by longin domain phosphorylation. |
Isoform-specific overexpression, L1CAM surface trafficking assay, phosphomimetic/phospho-null mutations, immunofluorescence |
International journal of molecular sciences |
Low |
38139155
|
| 2023 |
VAMP7 specifically co-distributes with CCL2-containing granules (but not TNFα- or histamine-containing granules) in bone marrow-derived mast cells, and VAMP7 knockdown markedly reduces CCL2 secretion after antigen stimulation, revealing VAMP7-dependent heterogeneous secretory regulation. |
siRNA knockdown, immunocytochemistry, confocal microscopy, CCL2 ELISA after antigen stimulation |
Biochemical and biophysical research communications |
Medium |
38029541
|
| 2026 |
VAMP7 knockout glioblastoma cells show impaired secretion of ER- and mitochondrial-derived proteins and signs of organellar stress; in a preclinical rat glioblastoma model, VAMP7 KO tumors are more necrotic with reduced macrophage infiltration, suggesting VAMP7-dependent late endosomal secretion serves as an organelle quality-control and stress-communication mechanism. |
VAMP7 KO cell lines, secretome proteomics, organellar stress markers, in vivo rat glioblastoma model, macrophage infiltration analysis |
Nature communications |
Medium |
41723185
|