The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion
Open accessAbstract
Activation of macrophages with lipopolysaccharide (LPS) induces the rapid synthesis and secretion of proinflammatory cytokines, such as tumor necrosis factor (TNFalpha), for priming the immune response. TNFalpha plays a key role in inflammatory disease; yet, little is known of the intracellular trafficking events leading to its secretion. In order to identify molecules involved in this secretory pathway, we asked whether any of the known trafficking proteins are regulated by LPS. We found that the levels of SNARE proteins were rapidly and significantly up- or downregulated during macrophage activation. A subset of t-SNAREs (Syntaxin 4/SNAP23/Munc18c) known to control regulated exocytosis in other cell types was substantially increased by LPS in a temporal pattern coinciding with peak TNFalpha secretion. Syntaxin 4 formed a complex with Munc18c at the cell surface of macrophages. Functional studies involving the introduction of Syntaxin 4 cDNA or peptides into macrophages implicate this t-SNARE in a rate-limiting step of TNFalpha secretion and in membrane ruffling during macrophage activation. We conclude that, in macrophages, SNAREs are regulated in order to accommodate the rapid onset of cytokine secretion and for membrane traffic associated with the phenotypic changes of immune activation. This represents a novel regulatory role for SNAREs in regulated secretion and in macrophage-mediated host defense.
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In macrophages, TNF is released to the extracellular milieu via the constitutive secretion pathway, and its trafficking is the best understood of all cytokines.
“In macrophages, TNF is released to the extracellular milieu via the constitutive secretion pathway, and its trafficking is the best understood of all cytokines (9, 17, 18).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [18]
The Stx4/SNAP23/VAMP3 complex facilitates the passage of TNF from recycling endosomes to the cell membrane.
“Thence, the Stx4/SNAP23/VAMP3 complex facilitates the passage of TNF from recycling endosomes to the cell membrane (17, 18).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [18]
LPS increases the expression of vesicle trafficking proteins that regulate TNF trafficking.
“Moreover, LPS was found to increase the expression of vesicle trafficking proteins that regulate TNF trafficking (17, 18).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [18]
The post-Golgi trafficking of IL-6 follows a route that is dependent on Stx6 and Vti1b, which form a complex with cognate SNARE VAMP3 at recycling endosomes.
“The post-Golgi trafficking of IL-6 follows a route that is also dependent on Stx6 and Vti1b, which form a complex with cognate SNARE VAMP3 at recycling endosomes (17, 18).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [18]
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“Upon activation, macrophages have been found to increase the level of a number of key SNARE proteins including Stx4 and VAMP3 (13,19,20).”
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“Data concerning TNF secretion after TLR4 receptor activation have been mainly generated in macrophages, where it is known to require the association of syntaxin-6 and -7 with VAMP3 (20) and the association of SNAP23 with syntaxin-4 (21), among other events (22).”
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“Members of the soluble Nethylmaleimide sensitive factor attachment protein receptor (SNARE) family have been shown to be involved in the intracellular vesicle transport in neurons and immune cells (38-42).”
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Syntaxin7 Is Required for Lytic Granule Release from Cytotoxic T Lymphocytes
Pattu, V., Qu, B., Marshall, M. R., Becherer, U., Junker, C., Matti, U., Schwarz, E. C., Krause, E., Hoth, M., & Rettig, J. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01193.x · Cited by 50 · see citing works
Stanley, A. C., Lieu, Z. Z., Wall, A. A., Venturato, J., Khromykh, T., Hamilton, N. A., Gleeson, P. A., & Stow, J. L. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0412191 · Cited by 55 · see citing works
“Immunofluorescence staining was performed as described previously [19]”
MethodSelf-citationOsuna-Jiménez, I., Williams, T., Prieto‐Álamo, M., Abril, N., Chipman, J. K., & Pueyo, C. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2009.02.020 · Cited by 48 · see citing works
“Our results are in agreement with previously reported changes in murine SNARE protein levels in response to LPS, accommodating the rapid onset of cytokine secretion and membrane traffic associated with the phenotypic changes of immune activation [42].”
ResultOxidized phagosomal NOX2 complex is replenished from lysosomes
Dingjan, I., Linders, P. T. A., van den Bekerom, L., Baranov, M. V., Halder, P., ter Beest, M., & van den Bogaart, G. (2017) · Journal of Cell Science · doi:10.1242/jcs.196931 · Cited by 47 · see citing works
“Although SNAP23 has long been considered to be a plasma membrane SNARE (Chamberlain and Gould, 2002; Hong, 2005; Kawanishi et al., 2000; Pagan et al., 2003; Paumet et al., 2000; Tellam et al., 1997; Volchuk et al., 1996; Wang et al., 2004), it is increasingly clear that it also has intracellular functions in many diff…”
BackgroundOxidized LDL immune complexes induce release of sphingosine kinase in human U937 monocytic cells
Hammad, S. M., Taha, T. A., Nareika, A., Johnson, K. R., Lopes-Virella, M. F., & Obeid, L. M. (2006) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2005.12.004 · Cited by 45 · see citing works
The SNARE VAMP7 Regulates Exocytic Trafficking of Interleukin-12 in Dendritic Cells
Chiaruttini, G., Piperno, G. M., Jouve, M. J., Nardi, F. D., Larghi, P., Peden, A. A., Baj, G., Müller, S., Valitutti, S., Galli, T., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.055 · Cited by 45 · see citing works
“Surface delivery of secretory proteins via vesicular SNARE requires a cognate PM acceptor complex constituted by the R-SNAREs SNAP23 and Syntaxin 4 in immune cells (Murray et al., 2005b; Pagan et al., 2003).”
BackgroundRab31 and APPL2 enhance FcγR-mediated phagocytosis through PI3K/Akt signaling in macrophages
Yeo, J. C., Wall, A. A., Luo, L., & Stow, J. L. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-10-1457 · Cited by 44 · see citing works
“Immunofluorescence, fluorescence microscopy, and live-cell imaging Immunofluorescence staining was performed as previously described (Pagan et al., 2003).”
MethodSelf-citationThe Exocytosis Regulator Synaptotagmin V Controls Phagocytosis in Macrophages
Vinet, A. F., Fukuda, M., & Descoteaux, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5289 · Cited by 42 · see citing works
Zhang, S., Ma, D., Wang, X., Celkan, T. T., Nordenskjöld, M., Henter, J., Fadeel, B., & Zheng, C. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07191.x · Cited by 41 · see citing works
“…fusion events have been implicated in the process of phagosome formation and maturation during phagocytosis (Hackam et al, 1996; Ward et al, 2000; Braun et al, 2004), as well as the regulation of macrophage secretion of cytokines (Pagan et al, 2003; Murray et al, 2005; Kay et al, 2006).”
BackgroundThe structural and functional evidence for vesicular release from astrocytes in situ
Bohmbach, K., Schwarz, M. K., Schoch, S., & Henneberger, C. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.01.015 · Cited by 42 · see citing works
Veale, K. J., Offenhäuser, C., Lei, N., Stanley, A. C., Stow, J. L., & Murray, R. Z. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.04.016 · Cited by 38 · see citing works
Self-citationSequential recruitment of Rab GTPases during early stages of phagocytosis
Yeo, J. C., Wall, A. A., Luo, L., & Stow, J. L. (2016) · Cellular Logistics · doi:10.1080/21592799.2016.1140615 · Cited by 36 · see citing works
Self-citationGabaev, I., Williamson, J. C., Crozier, T. W. M., Schulz, T. F., & Lehner, P. J. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108249 · Cited by 36 · see citing works
“Although the reason for their depletion by K5 is unclear, many members of the SNARE family are involved in cytokine (Collins et al., 2015; Naegelen et al., 2015; Pagan et al., 2003) and tumor necrosis factor alpha (TNF-a) secretion (STX7) (Murray et al., 2005).”
BackgroundRobust syntaxin-4 immunoreactivity in mammalian horizontal cell processes
Hirano, A. A., Brandstätter, J. H., VILA, A., & Brecha, N. C. (2007) · Visual Neuroscience · doi:10.1017/s0952523807070198 · Cited by 37 · see citing works
“…from cells in the immune system ~Stow et al., 2006!, such as crystalloid granules from eosinophils ~Logan et al., 2003!, several types of granules from neutrophils ~Logan et al., 2003!, degranulation of mast cells ~Blank et al., 2001!, and cytokine secretion from macrophages ~Pagan et al., 2003!.”
BackgroundNaegelen, I., Plançon, S., Nicot, N., Kaoma, T., Muller, A., Vallar, L., Tschirhart, E. J., & ́chard, S. B. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0514-254rr · Cited by 34 · see citing works
“For example, STX4 acts with VAMP3 in TNF secretion and phagocytosis in macrophages [37, 38], whereas these 2 proteins are involved in degranulation in mast cells [41–44].”
BackgroundSikorra, S., Litschko, C., Müller, C., Thiel, N., Galli, T., Eichner, T., & Binz, T. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.024 · Cited by 32 · see citing works
Verboogen, D. R. J., Mancha, N. G., ter Beest, M., & van den Bogaart, G. (2017) · eLife · doi:10.7554/elife.23525 · Cited by 32 · see citing works
“…muscle cells (Tellam et al., 1997; Hong, 2005), and are also implied in insulin secretion from pancreatic beta cells (Zhu et al., 2015), secretion of dense-core granules, a-granules and lysosomes from human platelets (Schraw et al., 2003) and TNFa secretion from macrophages (Pagan et al., 2003).”
BackgroundBoddul, S. V., Meng, J., Dolly, J. O., & Wang, J. (2013) · FEBS Journal · doi:10.1111/febs.12620 · Cited by 29 · see citing works
Haney, D., Quigley, M. F., Asher, T. E., Ambrozak, D. R., Emma Gostick, D., Price, D. A., Douek, D. C., & Betts, M. R. (2011) · Journal of Immunological Methods · doi:10.1016/j.jim.2011.04.003 · Cited by 26 · see citing works
“Importantly, the TNF-α Processing Inhibitor 0 (TAPI-0) can directly prevent TNF release from the cell surface (Crowe et al., 1995; Pagan et al., 2003; Huse et al., 2006), effectively trapping TNF on the surface of the producing cell.”
BackgroundMeng, J., Zou, X., Wu, R., Zhong, R., Zhu, D., & Zhang, Y. (2014) · Protein & Cell · doi:10.1007/s13238-014-0025-4 · Cited by 28 · see citing works
“In addition, a subset of t-SNAREs (syntaxin 4/SNAP23/Munc18c) performs a regulatory function in cytokine secretion in macrophages (Pagan, 2003).”
BackgroundLipopolysaccharides and Plant Innate Immunity
Erbs, G., Molinaro, A., Dow, J. M., & Newman, M. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-9078-2_17 · Cited by 26 · see citing works
Yu, C., Micaroni, M., Puyskens, A., Schultz, T. E., Yeo, J. C., Stanley, A. C., Lucas, M., Kurihara, J. N., Dobos, K. M., Stow, J. L., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500017 · Cited by 25 · see citing works
“RP105 macrophages by utilizing immunolabeling of surface TNF in cells treated with the TACE inhibitor, TAPI, followed by permeabilization and staining of intracellular TNF with a second round of immunolabeling using a different fluorophore (38) (Fig.”
MethodSelf-citationMedina‐Tamayo, J., Ibarra-Sánchez, A., Padilla-Trejo, A., & González‐Espinosa, C. (2010) · Inflammation Research · doi:10.1007/s00011-010-0230-4 · Cited by 25 · see citing works
“The second fusion process involves the VAMP3-containing recycling endosome and the t-SNARE complex at the plasma membrane comprising syntaxin 4 and SNAP-23 [28, 29].”
BackgroundA role for host cell exocytosis in InlB‐mediated internalisation of Listeria monocytogenes
Ngo, H. V., Bhalla, M., Chen, D.-Y., & Ireton, K. (2017) · Cellular Microbiology · doi:10.1111/cmi.12768 · Cited by 24 · see citing works
“Exofacial VAMP3‐GFP co‐localised with SNAP23 or Munc18‐1 around InlB‐coated beads (Figure S1b), consistent with the roles of these exocytic proteins in InlB‐mediated entry (Figures 1 and 2aii).”
BackgroundInfluentialInvolvement of Cathepsins in Innate and Adaptive Immune Responses in Periodontitis
Yan, X., Wu, Z., Wang, B., Yu, T., Hu, Y., Wang, S., Deng, C., Zhao, B., Nakanishi, H., & Zhang, X. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/4517587 · Cited by 24 · see citing works
The effect of natural products on inflammatory cytokines production and secretion
Barakat, M. M., Syed, N. K., Hasen, E., Abdulrazzaq, S. B., Thiab, S. H., Al‐Najjar, M. A. A., Omar, A., Lucy, T. T., Mamun-Or-Rashid, A. N. M., Yagi, M., et al. (2023) · Phytomedicine Plus · doi:10.1016/j.phyplu.2023.100488 · Cited by 24 · see citing works
Wild-type huntingtin regulates human macrophage function
O’Regan, G. C., Farag, S. H., Ostroff, G. R., Tabrizi, S. J., & André, R. (2020) · Scientific Reports · doi:10.1038/s41598-020-74042-8 · Cited by 22 · see citing works
An Emerging Role for SNARE Proteins in Dendritic Cell Function
Collins, L. E., DeCourcey, J., Luca, M. D., Rochfort, K. D., & Loscher, C. E. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00133 · Cited by 22 · see citing works
Membrane trafficking as an active regulator of constitutively secreted cytokines
Revelo, N. H., ter Beest, M., & van den Bogaart, G. (2019) · Journal of Cell Science · doi:10.1242/jcs.234781 · Cited by 22 · see citing works
“Interestingly, not only does their downregulation by RNAi or the overexpression of dominant-negative mutants lead to reduced secretion of TNF-α – but their overexpression has the opposite effect (Mori et al., 2011;Murray et al., 2005a,b; Pagan et al., 2003), indicating that the levels of these trafficking proteins can…”
BackgroundInfluentialLiaw, K., Gök, Ö., DeRidder, L. B., Kannan, S., & Kannan, R. M. (2018) · Journal of Nanoparticle Research · doi:10.1007/s11051-018-4219-1 · Cited by 20 · see citing works
“This was expected, as LPS activation has been shown to upregulate a variety of internalization pathways, including t-SNARE membrane trafficking, TLR4 endocytosis via clathrin and caveolae pathways, and fluid-phase pinocytosis in macrophages and astrocytes (Peppelenbosch et al. 1999; Pagan et al. 2003; Zanoni et al. 20…”
BackgroundRöhl, J., West, Z. E., Rudolph, M., Zaharia, A., Lonkhuyzen, D. R. V., Hickey, D. K., Semmler, A., & Murray, R. Z. (2019) · Traffic · doi:10.1111/tra.12675 · Cited by 20 · see citing works
“Knockdown of VAMP7 and VAMP8 using siRNA showed both R-SNAREs regulate transport of MT1-MMP and immunoprecipitation experiments show both R-SNAREs can bind to the surface Q-SNARE complex Stx4/SNAP23.”
BackgroundInfluentialThe Rho GTPase Rac1 is required for recycling endosome-mediated secretion of TNF in macrophages
Stanley, A. C., Wong, C. X., Micaroni, M., Venturato, J., Khromykh, T., Stow, J. L., & Lacy, P. (2014) · Immunology & Cell Biology · doi:10.1038/icb.2013.90 · Cited by 21 · see citing works
Self-citationDistinct Roles for APPL1 and APPL2 in Regulating Toll‐like Receptor 4 Signaling in Macrophages
Yeo, J. C., Wall, A. A., Luo, L., Condon, N. D., & Stow, J. L. (2016) · Traffic · doi:10.1111/tra.12415 · Cited by 18 · see citing works
“Immunofluorescence, fluorescence microscopy and live cell imaging Immunofluorescence staining was performed as previously described (34).”
MethodSelf-citationExpression and transcriptional regulation of Munc18 isoforms in mast cells
Nigam, R., Sepulveda, J. L., Tuvim, M. J., Petrova, Y., Adachi, R., Dickey, B. F., & Agrawal, A. (2005) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2005.01.018 · Cited by 17 · see citing works
Dyer, R. P., Isoda, H. M., Salcedo, G. S., Speciale, G., Fletcher, M. H., Le, L. Q., Liu, Y., Brami‐Cherrier, K., Malik, S. Z., Vazquez-Cintron, E. J., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-13617-z · Cited by 15 · see citing works
West, Z. E., Aitcheson, S. M., Semmler, A., & Murray, R. Z. (2021) · Traffic · doi:10.1111/tra.12813 · Cited by 15 · see citing works
“5-fold by 12 hours post LPS stimulation (Figure 3F and Figure S3).(14) Together these results suggest that the VAMP4/Stx6/Stx7/Vti1b trans-SNARE complex regulates transport of MT1-MMP from the Golgi complex to late endosomes/lysosomes and that VAMP4, Vti1b and Stx6 are up-regulated to increase formation of this comple…”
BackgroundHuman monocytes store and secrete preformed CCL5, independent of de novo protein synthesis
Persaud, A. T., Bennett, S. A., Thaya, L., Burnie, J., & Guzzo, C. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.3a0820-522rr · Cited by 14 · see citing works
Functions of the Plant Qbc SNARE SNAP25 in Cytokinesis and Biotic and Abiotic Stress Responses.
Won, K., & Kim, H. (2020) · PubMed Central · doi:10.14348/molcells.2020.2245 · Cited by 14 · see citing works
“SNAP23 proteins play a pivotal role in immune cells by mediating the secretion of cytokines, antibodies, and granules (Pagan et al., 2003; Reales et al., 2005; Mollinedo et al., 2006).”
BackgroundChai, Y., Huang, X., Cong, B., Liu, S., Chen, K., Li, G., & Gaisano, H. Y. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.138 · Cited by 14 · see citing works
The role of the recycling endosome in regulating lamellipodia formation and macrophage migration
Veale, K. J., Offenhäuser, C., & Murray, R. Z. (2011) · Communicative & Integrative Biology · doi:10.4161/cib.13569 · Cited by 14 · see citing works
Platelet granule secretion mechanisms: Are they modified in sepsis?
Xu, X., & Sun, B. (2015) · Thrombosis Research · doi:10.1016/j.thromres.2015.09.008 · Cited by 13 · see citing works
Duque, G. A., Dion, R., Matte, C., Fabié, A., Descoteaux, J., Stäger, S., & Descoteaux, A. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100258 · Cited by 11 · see citing works
Salinas, E., Quintanar‐Stephano, A., Córdova-Dávalos, L. E., & Ouintanar, J. L. (2008) · PubMed · Cited by 11 · see citing works
Weimershaus, M., Carvalho, C., Rignault‐Bricard, R., Waeckel-Énée, E., Dussiot, M., Endert, P. V., Maciel, T. T., & Hermine, O. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.01.014 · Cited by 10 · see citing works
Syntaxin-4 is essential for IgE secretion by plasma cells
Rahman, A., DeCourcey, J., Larbi, N. B., Loughran, S. T., Walls, D., & Loscher, C. E. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.058 · Cited by 10 · see citing works
Patients and mice with deficiency in the SNARE protein SYNTAXIN-11 have a secondary B cell defect
Kögl, T., Chang, H., Staniek, J., Chiang, S. C. C., Thoulass, G., Lao, J., Weißert, K., Dettmer‐Monaco, V., Geiger, K., Manna, P. T., et al. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20221122 · Cited by 9 · see citing works
“The involvement of STX11 in the transport of cytokines is likely, since other SNARE proteins like STX4 regulate TNF α secretion by macrophages and STX3 is important for IL-6 secretion by DCs (Pagan et al., 2003; Collins et al., 2015; Stanley and Lacy, 2010; Murray and Stow, 2014).”
BackgroundRecombinant expression of Munc18c in a baculovirus system and interaction with syntaxin4
Hu, S., Gee, C. L., Latham, C. F., Rowlinson, S. W., Rova, U., Jones, A., Halliday, J. A., Bryant, N. J., James, D. E., & Martin, J. L. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(03)00197-9 · Cited by 9 · see citing works
Self-citationCastañeda-Ramírez, A., González-Rodríguez, D., Ja, H.-P., & Verdugo-Rodríguez, A. (2015) · PubMed Central · Cited by 9 · see citing works
Syntaxin-2 balances phagocytic uptake and phagolysosomal clearance in macrophages
Samanta, S., Nandi, A., Datta, R., & Dolai, S. (2025) · Journal of Cell Science · doi:10.1242/jcs.263855 · Cited by 8 · see citing works
Engineering an Effective Human SNAP-23 Cleaving Botulinum Neurotoxin A Variant
Sikorra, S., Donald, S., Elliott, M. A., Schwede, S., Coker, S.-F., Kupinski, A. P., Tripathi, V., Keith, F., Beard, M., & Binz, T. (2020) · Toxins · doi:10.3390/toxins12120804 · Cited by 8 · see citing works
- Authors
- Pagan, J. K., Wylie, F. G., Joseph, S., Widberg, C., Bryant, N. J., James, D. E., & Stow, J. L.
- Affiliations
- The University of Queensland (AU)
- Institute for Molecular Bioscience (AU)
- Garvan Institute of Medical Research (AU)
- Corresponding author
- Stow, Jennifer L
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2003-01
- Volume
- 13
- Issue
- 2
- Pages
- 156-160
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2155132039
- Cited by
- 130
- References
- 28
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 11 · 2023: 3 · 2022: 2 · 2021: 5 · 2020: 6 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 9 · 2014: 8 · 2013: 7 · 2012: 7
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3850 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- syntaxin 4, macrophage activation, lipopolysaccharide, TNF-alpha secretion, regulated exocytosis, membrane traffic, Munc18c, SNAP23, cytokine production, ruffles
- MeSH terms
- Animals, Cell Line, Cell Membrane, Lipopolysaccharides, Macrophage Activation, Membrane Proteins, Tumor Necrosis Factor-alpha, Cytokines, Vesicular Transport Proteins, SNARE Proteins, Qa-SNARE Proteins, Mice
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