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Journal articles on the topic 'TI-VAMP'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Alberts, Philipp, Rachel Rudge, Ina Hinners, Aude Muzerelle, Sonia Martinez-Arca, Theano Irinopoulou, Véronique Marthiens, et al. "Cross Talk between Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein-mediated Transport and L1-mediated Adhesion." Molecular Biology of the Cell 14, no. 10 (October 2003): 4207–20. http://dx.doi.org/10.1091/mbc.e03-03-0147.

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The membrane-trafficking pathway mediated by tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) in neurons is still unknown. We show herein that TI-VAMP expression is necessary for neurite outgrowth in PC12 cells and hippocampal neurons in culture. TI-VAMP interacts with plasma membrane and endosomal target soluble N-ethylmaleimide-sensitive factor attachment protein receptors, suggesting that TI-VAMP mediates a recycling pathway. L1, a cell-cell adhesion molecule involved in axonal outgrowth, colocalized with TI-VAMP in the developing brain, neurons in culture, and PC12 cells. Plasma membrane L1 was internalized into the TI-VAMP–containing compartment. Silencing of TI-VAMP resulted in reduced expression of L1 at the plasma membrane. Finally, using the extracellular domain of L1 and N-cadherin immobilized on beads, we found that the silencing of TI-VAMP led to impaired L1- but not N-cadherin–mediated adhesion. Furthermore, TI-VAMP- but not synaptobrevin 2-containing vesicles accumulated at the site of the L1 bead-cell junction. We conclude that TI-VAMP mediates the intracellular transport of L1 and that L1-mediated adhesion controls this membrane trafficking, thereby suggesting an important cross talk between membrane trafficking and cell-cell adhesion.

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2

Alberts, Philipp, Rachel Rudge, Theano Irinopoulou, Lydia Danglot, Cécile Gauthier-Rouvière, and Thierry Galli. "Cdc42 and Actin Control Polarized Expression of TI-VAMP Vesicles to Neuronal Growth Cones and Their Fusion with the Plasma Membrane." Molecular Biology of the Cell 17, no. 3 (March 2006): 1194–203. http://dx.doi.org/10.1091/mbc.e05-07-0643.

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Tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP)-mediated fusion of intracellular vesicles with the plasma membrane is crucial for neurite outgrowth, a pathway not requiring synaptobrevin-dependent exocytosis. Yet, it is not known how the TI-VAMP membrane trafficking pathway is regulated or how it is coordinated with cytoskeletal dynamics within the growth cone that guide neurite outgrowth. Here, we demonstrate that TI-VAMP, but not synaptobrevin 2, concentrates in the peripheral, F-actin-rich region of the growth cones of hippocampal neurons in primary culture. Its accumulation correlates with and depends upon the presence of F-actin. Moreover, acute stimulation of actin remodeling by homophilic activation of the adhesion molecule L1 induces a site-directed, actin-dependent recruitment of the TI-VAMP compartment. Expression of a dominant-positive mutant of Cdc42, a key regulator of cell polarity, stimulates formation of F-actin- and TI-VAMP-rich filopodia outside the growth cone. Furthermore, we report that Cdc42 activates exocytosis of pHLuorin tagged TI-VAMP in an actin-dependent manner. Collectively, our data suggest that Cdc42 and regulated assembly of the F-actin network control the accumulation and exocytosis of TI-VAMP-containing membrane vesicles in growth cones to coordinate membrane trafficking and actin remodeling during neurite outgrowth.

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3

Martinez-Arca, Sonia, Philipp Alberts, Ahmed Zahraoui, Daniel Louvard, and Thierry Galli. "Role of Tetanus Neurotoxin Insensitive Vesicle-Associated Membrane Protein (Ti-Vamp) in Vesicular Transport Mediating Neurite Outgrowth." Journal of Cell Biology 149, no. 4 (May 15, 2000): 889–900. http://dx.doi.org/10.1083/jcb.149.4.889.

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How vesicular transport participates in neurite outgrowth is still poorly understood. Neurite outgrowth is not sensitive to tetanus neurotoxin thus does not involve synaptobrevin-mediated vesicular transport to the plasma membrane of neurons. Tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) is a vesicle-SNARE (soluble N-ethylmaleimide-sensitive fusion protein [NSF] attachment protein [SNAP] receptor), involved in transport to the apical plasma membrane in epithelial cells, a tetanus neurotoxin-resistant pathway. Here we show that TI-VAMP is essential for vesicular transport-mediating neurite outgrowth in staurosporine-differentiated PC12 cells. The NH2-terminal domain, which precedes the SNARE motif of TI-VAMP, inhibits the association of TI-VAMP with synaptosome-associated protein of 25 kD (SNAP25). Expression of this domain inhibits neurite outgrowth as potently as Botulinum neurotoxin E, which cleaves SNAP25. In contrast, expression of the NH2-terminal deletion mutant of TI-VAMP increases SNARE complex formation and strongly stimulates neurite outgrowth. These results provide the first functional evidence for the role of TI-VAMP in neurite outgrowth and point to its NH2-terminal domain as a key regulator in this process.

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4

Galli, Thierry, Ahmed Zahraoui, Vadakkanchery V. Vaidyanathan, Graça Raposo, Jian Min Tian, Michael Karin, Heiner Niemann, and Daniel Louvard. "A Novel Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein in SNARE Complexes of the Apical Plasma Membrane of Epithelial Cells." Molecular Biology of the Cell 9, no. 6 (June 1998): 1437–48. http://dx.doi.org/10.1091/mbc.9.6.1437.

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The importance of soluble N-ethyl maleimide (NEM)-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (SNAREs) in synaptic vesicle exocytosis is well established because it has been demonstrated that clostridial neurotoxins (NTs) proteolyze the vesicle SNAREs (v-SNAREs) vesicle-associated membrane protein (VAMP)/brevins and their partners, the target SNAREs (t-SNAREs) syntaxin 1 and SNAP25. Yet, several exocytotic events, including apical exocytosis in epithelial cells, are insensitive to numerous clostridial NTs, suggesting the presence of SNARE-independent mechanisms of exocytosis. In this study we found that syntaxin 3, SNAP23, and a newly identified VAMP/brevin, tetanus neurotoxin (TeNT)-insensitive VAMP (TI-VAMP), are insensitive to clostridial NTs. In epithelial cells, TI-VAMP–containing vesicles were concentrated in the apical domain, and the protein was detected at the apical plasma membrane by immunogold labeling on ultrathin cryosections. Syntaxin 3 and SNAP23 were codistributed at the apical plasma membrane where they formed NEM-dependent SNARE complexes with TI-VAMP and cellubrevin. We suggest that TI-VAMP, SNAP23, and syntaxin 3 can participate in exocytotic processes at the apical plasma membrane of epithelial cells and, more generally, domain-specific exocytosis in clostridial NT-resistant pathways.

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5

Randhawa, Varinder K., Farah S. L. Thong, Dawn Y. Lim, Dailin Li, Rami R. Garg, Rachel Rudge, Thierry Galli, Assaf Rudich, and Amira Klip. "Insulin and Hypertonicity Recruit GLUT4 to the Plasma Membrane of Muscle Cells by Using N-Ethylmaleimide-sensitive Factor-dependent SNARE Mechanisms but Different v-SNAREs: Role of TI-VAMP." Molecular Biology of the Cell 15, no. 12 (December 2004): 5565–73. http://dx.doi.org/10.1091/mbc.e04-03-0266.

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Insulin and hypertonicity each increase the content of GLUT4 glucose transporters at the surface of muscle cells. Insulin enhances GLUT4 exocytosis without diminishing its endocytosis. The insulin but not the hypertonicity response is reduced by tetanus neurotoxin, which cleaves vesicle-associated membrane protein (VAMP)2 and VAMP3, and is rescued upon introducing tetanus neurotoxin-resistant VAMP2. Here, we show that hypertonicity enhances GLUT4 recycling, compounding its previously shown ability to reduce GLUT4 endocytosis. To examine whether the canonical soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) mechanism is required for the plasma membrane fusion of the tetanus neurotoxin-insensitive GLUT4 vesicles, L6 myoblasts stably expressing myc-tagged GLUT4 (GLUT4myc) were transiently transfected with dominant negative N-ethylmaleimide-sensitive factor (NSF) (DN-NSF) or small-interfering RNA to tetanus neurotoxin-insensitive VAMP (TI-VAMP siRNA). Both strategies markedly reduced the basal level of surface GLUT4myc and the surface gain of GLUT4myc in response to hypertonicity. The insulin effect was abolished by DN-NSF, but only partly reduced by TI-VAMP siRNA. We propose that insulin and hypertonicity recruit GLUT4myc from partly overlapping, but distinct sources defined by VAMP2 and TI-VAMP, respectively.

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6

Ren, Qiansheng, Holly Kalani Barber, Garland L. Crawford, Zubair A. Karim, Chunxia Zhao, Wangsun Choi, Cheng-Chun Wang, Wanjin Hong, and Sidney W. Whiteheart. "Endobrevin/VAMP-8 Is the Primary v-SNARE for the Platelet Release Reaction." Molecular Biology of the Cell 18, no. 1 (January 2007): 24–33. http://dx.doi.org/10.1091/mbc.e06-09-0785.

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Platelet secretion is critical to hemostasis. Release of granular cargo is mediated by soluble NSF attachment protein receptors (SNAREs), but despite consensus on t-SNAREs usage, it is unclear which Vesicle Associated Membrane Protein (VAMPs: synaptobrevin/VAMP-2, cellubrevin/VAMP-3, TI-VAMP/VAMP-7, and endobrevin/VAMP-8) is required. We demonstrate that VAMP-8 is required for release from dense core granules, alpha granules, and lysosomes. Platelets from VAMP-8−/−mice have a significant defect in agonist-induced secretion, though signaling, morphology, and cargo levels appear normal. In contrast, VAMP-2+/−, VAMP-3−/−, and VAMP-2+/−/VAMP-3−/−platelets showed no defect. Consistently, tetanus toxin had no effect on secretion from permeabilized mouse VAMP-3−/−platelets or human platelets, despite cleavage of VAMP-2 and/or -3. Tetanus toxin does block the residual release from permeabilized VAMP-8−/−platelets, suggesting a secondary role for VAMP-2 and/or -3. These data imply a ranked redundancy of v-SNARE usage in platelets and suggest that VAMP-8−/−mice will be a useful in vivo model to study platelet exocytosis in hemostasis and vascular inflammation.

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7

Rao, Swathi K., Chau Huynh, Veronique Proux-Gillardeaux, Thierry Galli, and Norma W. Andrews. "Identification of SNAREs Involved in Synaptotagmin VII-regulated Lysosomal Exocytosis." Journal of Biological Chemistry 279, no. 19 (March 1, 2004): 20471–79. http://dx.doi.org/10.1074/jbc.m400798200.

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Ca2+-regulated exocytosis of lysosomes has been recognized recently as a ubiquitous process, important for the repair of plasma membrane wounds. Lysosomal exocytosis is regulated by synaptotagmin VII, a member of the synaptotagmin family of Ca2+-binding proteins localized on lysosomes. Here we show that Ca2+-dependent interaction of the synaptotagmin VII C2A domain with SNAP-23 is facilitated by syntaxin 4. Specific interactions also occurred in cell lysates between the plasma membrane t-SNAREs SNAP-23 and syntaxin 4 and the lysosomal v-SNARE TI-VAMP/VAMP7. Following cytosolic Ca2+elevation, SDS-resistant complexes containing SNAP-23, syntaxin 4, and TI-VAMP/VAMP7 were detected on membrane fractions. Lysosomal exocytosis was inhibited by the SNARE domains of syntaxin 4 and TI-VAMP/VAMP7 and by cleavage of SNAP-23 with botulinum neurotoxin E, thereby functionally implicating these SNAREs in Ca2+-regulated exocytosis of conventional lysosomes.

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8

Steffen, Anika, Gaëlle Le Dez, Renaud Poincloux, Chiara Recchi, Pierre Nassoy, Klemens Rottner, Thierry Galli, and Philippe Chavrier. "MT1-MMP-Dependent Invasion Is Regulated by TI-VAMP/VAMP7." Current Biology 18, no. 12 (June 2008): 926–31. http://dx.doi.org/10.1016/j.cub.2008.05.044.

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9

Vivona, Sandro, Corey W. Liu, Pavel Strop, Valeria Rossi, Francesco Filippini, and Axel T. Brunger. "The Longin SNARE VAMP7/TI-VAMP Adopts a Closed Conformation." Journal of Biological Chemistry 285, no. 23 (April 8, 2010): 17965–73. http://dx.doi.org/10.1074/jbc.m110.120972.

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10

Danglot, L., K. Zylbersztejn, M. Petkovic, M. Gauberti, H. Meziane, R. Combe, M. F. Champy, et al. "Absence of TI-VAMP/Vamp7 Leads to Increased Anxiety in Mice." Journal of Neuroscience 32, no. 6 (February 8, 2012): 1962–68. http://dx.doi.org/10.1523/jneurosci.4436-11.2012.

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11

Danglot, L., M. Chaineau, M. Dahan, M. C. Gendron, N. Boggetto, F. Perez, and T. Galli. "Role of TI-VAMP and CD82 in EGFR cell-surface dynamics and signaling." Journal of Cell Science 123, no. 5 (February 9, 2010): 723–35. http://dx.doi.org/10.1242/jcs.062497.

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12

Danglot, L., M. Chaineau, M. Dahan, M. C. Gendron, N. Boggetto, F. Perez, and T. Galli. "Role of TI-VAMP and CD82 in EGFR cell-surface dynamics and signaling." Development 137, no. 6 (February 23, 2010): e1-e1. http://dx.doi.org/10.1242/dev.050500.

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13

Braun, Virginie, Vincent Fraisier, Graça Raposo, Ilse Hurbain, Jean-Baptiste Sibarita, Philippe Chavrier, Thierry Galli, and Florence Niedergang. "TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles in macrophages." EMBO Journal 23, no. 21 (October 7, 2004): 4166–76. http://dx.doi.org/10.1038/sj.emboj.7600427.

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14

Sato, Mahito, Shinichiro Yoshimura, Rika Hirai, Ayako Goto, Masataka Kunii, Nur Atik, Takashi Sato, et al. "The Role of VAMP7/TI-VAMP in Cell Polarity and Lysosomal Exocytosis in vivo." Traffic 12, no. 10 (August 5, 2011): 1383–93. http://dx.doi.org/10.1111/j.1600-0854.2011.01247.x.

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15

Sikorra, Stefan, Tina Henke, Subramanyam Swaminathan, Thierry Galli, and Thomas Binz. "Identification of the Amino Acid Residues Rendering TI-VAMP Insensitive toward Botulinum Neurotoxin B." Journal of Molecular Biology 357, no. 2 (March 2006): 574–82. http://dx.doi.org/10.1016/j.jmb.2005.12.075.

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16

Chaineau, Mathilde, Lydia Danglot, and Thierry Galli. "Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking." FEBS Letters 583, no. 23 (October 16, 2009): 3817–26. http://dx.doi.org/10.1016/j.febslet.2009.10.026.

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17

Martinez-Arca, S. "Ectopic expression of syntaxin 1 in the ER redirects TI-VAMP- and cellubrevin-containing vesicles." Journal of Cell Science 116, no. 13 (May 20, 2003): 2805–16. http://dx.doi.org/10.1242/jcs.00467.

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18

Proux-Gillardeaux, Véronique, Graça Raposo, Theano Irinopoulou, and Thierry Galli. "Expression of the Longin domain of TI-VAMP impairs lysosomal secretion and epithelial cell migration." Biology of the Cell 99, no. 5 (May 2007): 261–71. http://dx.doi.org/10.1042/bc20060097.

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19

Burgo, Andrea, Emmanuel Sotirakis, Marie‐Christine Simmler, Agathe Verraes, Christophe Chamot, Jeremy C. Simpson, Letizia Lanzetti, Véronique Proux‐Gillardeaux, and Thierry Galli. "Role of Varp, a Rab21 exchange factor and TI‐VAMP/VAMP7 partner, in neurite growth." EMBO reports 10, no. 10 (September 11, 2009): 1117–24. http://dx.doi.org/10.1038/embor.2009.186.

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20

Verderio, Claudia, Cinzia Cagnoli, Matteo Bergami, Maura Francolini, Ursula Schenk, Alessio Colombo, Loredana Riganti, et al. "TI-VAMP/VAMP7 is the SNARE of secretory lysosomes contributing to ATP secretion from astrocytes." Biology of the Cell 104, no. 4 (January 11, 2012): 213–28. http://dx.doi.org/10.1111/boc.201100070.

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21

Fuschini, Giulia, Tiziana Cotrufo, Oriol Ros, Ashraf Muhaisen, Rosa Andrés, Joan X. Comella, and Eduardo Soriano. "Syntaxin-1/TI-VAMP SNAREs interact with Trk receptors and are required for neurotrophin-dependent outgrowth." Oncotarget 9, no. 89 (November 13, 2018): 35922–40. http://dx.doi.org/10.18632/oncotarget.26307.

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22

Burgo, Andrea, Véronique Proux-Gillardeaux, Emmanuel Sotirakis, Philippe Bun, Alessandra Casano, Agathe Verraes, Ronald K. H. Liem, Etienne Formstecher, Maïté Coppey-Moisan, and Thierry Galli. "A Molecular Network for the Transport of the TI-VAMP/VAMP7 Vesicles from Cell Center to Periphery." Developmental Cell 23, no. 1 (July 2012): 166–80. http://dx.doi.org/10.1016/j.devcel.2012.04.019.

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23

Fader, Claudio Marcelo, Diego Germán Sánchez, María Belén Mestre, and María Isabel Colombo. "TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 12 (December 2009): 1901–16. http://dx.doi.org/10.1016/j.bbamcr.2009.09.011.

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24

Burgo, Andrea, Alessandra M. Casano, Aurelia Kuster, Stefan T. Arold, Guan Wang, Sébastien Nola, Agathe Verraes, Florent Dingli, Damarys Loew, and Thierry Galli. "Increased activity of the Vesicular SolubleN-Ethylmaleimide-sensitive Factor Attachment Protein Receptor TI-VAMP/VAMP7 by Tyrosine Phosphorylation in the Longin Domain." Journal of Biological Chemistry 288, no. 17 (March 7, 2013): 11960–72. http://dx.doi.org/10.1074/jbc.m112.415075.

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25

Vacca, Marcella, Lara Albania, Floriana Della Ragione, Andrea Carpi, Valeria Rossi, Maria Strazzullo, Nicola De Franceschi, Ornella Rossetto, Francesco Filippini, and Maurizio D'Esposito. "Alternative splicing of the human gene SYBL1 modulates protein domain architecture of longin VAMP7/TI-VAMP, showing both non-SNARE and synaptobrevin-like isoforms." BMC Molecular Biology 12, no. 1 (May 24, 2011). http://dx.doi.org/10.1186/1471-2199-12-26.

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