9 results on '"Galli T"'
Search Results
2. Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.
- Author
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Galli, T, primary, Chilcote, T, additional, Mundigl, O, additional, Binz, T, additional, Niemann, H, additional, and De Camilli, P, additional
- Published
- 1994
- Full Text
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3. BLOC-1 and BLOC-3 regulate VAMP7 cycling to and from melanosomes via distinct tubular transport carriers.
- Author
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Dennis MK, Delevoye C, Acosta-Ruiz A, Hurbain I, Romao M, Hesketh GG, Goff PS, Sviderskaya EV, Bennett DC, Luzio JP, Galli T, Owen DJ, Raposo G, and Marks MS
- Subjects
- Animals, Cell Membrane metabolism, Cell Membrane ultrastructure, Green Fluorescent Proteins metabolism, Humans, Intracellular Signaling Peptides and Proteins, Melanocytes metabolism, Melanocytes ultrastructure, Melanosomes ultrastructure, Membrane Glycoproteins metabolism, Mice, Inbred C57BL, Mitochondrial Proteins, Oxidoreductases metabolism, Pigmentation, Protein Transport, Qa-SNARE Proteins metabolism, Recombinant Fusion Proteins metabolism, Transport Vesicles ultrastructure, rab GTP-Binding Proteins metabolism, Carrier Proteins metabolism, Endocytosis, Lectins metabolism, Melanosomes metabolism, Nerve Tissue Proteins metabolism, R-SNARE Proteins metabolism, Transport Vesicles metabolism
- Abstract
Endomembrane organelle maturation requires cargo delivery via fusion with membrane transport intermediates and recycling of fusion factors to their sites of origin. Melanosomes and other lysosome-related organelles obtain cargoes from early endosomes, but the fusion machinery involved and its recycling pathway are unknown. Here, we show that the v-SNARE VAMP7 mediates fusion of melanosomes with tubular transport carriers that also carry the cargo protein TYRP1 and that require BLOC-1 for their formation. Using live-cell imaging, we identify a pathway for VAMP7 recycling from melanosomes that employs distinct tubular carriers. The recycling carriers also harbor the VAMP7-binding scaffold protein VARP and the tissue-restricted Rab GTPase RAB38. Recycling carrier formation is dependent on the RAB38 exchange factor BLOC-3. Our data suggest that VAMP7 mediates fusion of BLOC-1-dependent transport carriers with melanosomes, illuminate SNARE recycling from melanosomes as a critical BLOC-3-dependent step, and likely explain the distinct hypopigmentation phenotypes associated with BLOC-1 and BLOC-3 deficiency in Hermansky-Pudlak syndrome variants., (© 2016 Dennis et al.)
- Published
- 2016
- Full Text
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4. The vesicular SNARE Synaptobrevin is required for Semaphorin 3A axonal repulsion.
- Author
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Zylbersztejn K, Petkovic M, Burgo A, Deck M, Garel S, Marcos S, Bloch-Gallego E, Nothias F, Serini G, Bagnard D, Binz T, and Galli T
- Subjects
- Animals, COS Cells, Chlorocebus aethiops, Corpus Callosum anatomy & histology, Exocytosis physiology, Growth Cones physiology, Mice, Mice, Knockout, R-SNARE Proteins genetics, R-SNARE Proteins metabolism, Semaphorin-3A metabolism, Signal Transduction, Vesicle-Associated Membrane Protein 2 genetics, Vesicle-Associated Membrane Protein 2 metabolism, Axons physiology, R-SNARE Proteins physiology, Semaphorin-3A physiology, Vesicle-Associated Membrane Protein 2 physiology
- Abstract
Attractive and repulsive molecules such as Semaphorins (Sema) trigger rapid responses that control the navigation of axonal growth cones. The role of vesicular traffic in axonal guidance is still largely unknown. The exocytic vesicular soluble N-ethylmaleimide sensitive fusion protein attachment protein receptor (SNARE) Synaptobrevin 2 (Syb2) is known for mediating neurotransmitter release in mature neurons, but its potential role in axonal guidance remains elusive. Here we show that Syb2 is required for Sema3A-dependent repulsion but not Sema3C-dependent attraction in cultured neurons and in the mouse brain. Syb2 associated with Neuropilin 1 and Plexin A1, two essential components of the Sema3A receptor, via its juxtatransmembrane domain. Sema3A receptor and Syb2 colocalize in endosomal membranes. Moreover, upon Sema3A treatment, Syb2-deficient neurons failed to collapse and transport Plexin A1 to cell bodies. Reconstitution of Sema3A receptor in nonneuronal cells revealed that Sema3A further inhibited the exocytosis of Syb2. Therefore, Sema3A-mediated signaling and axonal repulsion require Syb2-dependent vesicular traffic.
- Published
- 2012
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5. v-SNARE cellubrevin is required for basolateral sorting of AP-1B-dependent cargo in polarized epithelial cells.
- Author
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Fields IC, Shteyn E, Pypaert M, Proux-Gillardeaux V, Kang RS, Galli T, and Fölsch H
- Subjects
- Adaptor Protein Complex 1 genetics, Adaptor Protein Complex beta Subunits genetics, Animals, Cell Line, Cell Membrane metabolism, Cell Polarity drug effects, Dogs, Epithelial Cells cytology, Humans, Membrane Fusion drug effects, Membrane Fusion physiology, Metalloendopeptidases pharmacology, Protein Transport drug effects, Protein Transport physiology, Qa-SNARE Proteins genetics, Qa-SNARE Proteins metabolism, Receptors, LDL metabolism, SNARE Proteins genetics, Tetanus Toxin pharmacology, Vesicle-Associated Membrane Protein 3 genetics, Adaptor Protein Complex 1 metabolism, Adaptor Protein Complex beta Subunits metabolism, Cell Polarity physiology, Endosomes metabolism, Epithelial Cells metabolism, SNARE Proteins metabolism, Vesicle-Associated Membrane Protein 3 metabolism
- Abstract
The epithelial cell-specific adaptor complex AP-1B is crucial for correct delivery of many transmembrane proteins from recycling endosomes to the basolateral plasma membrane. Subsequently, membrane fusion is dependent on the formation of complexes between SNARE proteins located at the target membrane and on transport vesicles. Although the t-SNARE syntaxin 4 has been localized to the basolateral membrane, the v-SNARE operative in the AP-1B pathway remained unknown. We show that the ubiquitously expressed v-SNARE cellubrevin localizes to the basolateral membrane and to recycling endosomes, where it colocalizes with AP-1B. Furthermore, we demonstrate that cellubrevin coimmunoprecipitates preferentially with syntaxin 4, implicating this v-SNARE in basolateral fusion events. Cleavage of cellubrevin with tetanus neurotoxin (TeNT) results in scattering of AP-1B localization and missorting of AP-1B-dependent cargos, such as transferrin receptor and a truncated low-density lipoprotein receptor, LDLR-CT27. These data suggest that cellubrevin and AP-1B cooperate in basolateral membrane trafficking.
- Published
- 2007
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6. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform.
- Author
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Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, and Johannes L
- Subjects
- Animals, Biological Transport, Active, CHO Cells, Cricetinae, HeLa Cells, Humans, Protein Isoforms metabolism, Qa-SNARE Proteins, Qb-SNARE Proteins, SNARE Proteins, Shiga Toxins metabolism, Syntaxin 16, Vesicle-Associated Membrane Protein 3, Carrier Proteins metabolism, Endosomes metabolism, Membrane Proteins metabolism, Vesicular Transport Proteins, rab GTP-Binding Proteins metabolism, trans-Golgi Network metabolism
- Abstract
The molecular mechanisms underlying early/recycling endosomes-to-TGN transport are still not understood. We identified interactions between the TGN-localized putative t-SNAREs syntaxin 6, syntaxin 16, and Vti1a, and two early/recycling endosomal v-SNAREs, VAMP3/cellubrevin, and VAMP4. Using a novel permeabilized cell system, these proteins were functionally implicated in the post-Golgi retrograde transport step. The function of Rab6a' was also required, whereas its closely related isoform, Rab6a, has previously been implicated in Golgi-to-endoplasmic reticulum transport. Thus, our study shows that membrane exchange between the early endocytic and the biosynthetic/secretory pathways involves specific components of the Rab and SNARE machinery, and suggests that retrograde transport between early/recycling endosomes and the endoplasmic reticulum is critically dependent on the sequential action of two members of the Rab6 subfamily.
- Published
- 2002
- Full Text
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7. Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network.
- Author
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Wilcke M, Johannes L, Galli T, Mayau V, Goud B, and Salamero J
- Subjects
- HeLa Cells, Histocompatibility Antigens Class II metabolism, Humans, Intracellular Membranes metabolism, Melanoma, Experimental, Membrane Glycoproteins metabolism, Mutation, Neoplasm Proteins metabolism, Receptor, IGF Type 2 metabolism, Receptors, Transferrin metabolism, Shiga Toxin metabolism, Sialyltransferases metabolism, Cell Compartmentation, Endosomes metabolism, Glycoproteins, Membrane Proteins, Protein Transport physiology, rab GTP-Binding Proteins metabolism, trans-Golgi Network metabolism
- Abstract
Several GTPases of the Rab family, known to be regulators of membrane traffic between organelles, have been described and localized to various intracellular compartments. Rab11 has previously been reported to be associated with the pericentriolar recycling compartment, post-Golgi vesicles, and the trans-Golgi network (TGN). We compared the effect of overexpression of wild-type and mutant forms of Rab11 on the different intracellular transport steps in the endocytic/degradative and the biosynthetic/exocytic pathways in HeLa cells. We also studied transport from endosomes to the Golgi apparatus using the Shiga toxin B subunit (STxB) and TGN38 as reporter molecules. Overexpression of both Rab11 wild-type (Rab11wt) and mutants altered the localization of the transferrrin receptor (TfR), internalized Tf, the STxB, and TGN38. In cells overexpressing Rab11wt and in a GTPase-deficient Rab11 mutant (Rab11Q70L), these proteins were found in vesicles showing characteristics of sorting endosomes lacking cellubrevin (Cb). In contrast, they were redistributed into an extended tubular network, together with Cb, in cells overexpressing a dominant negative mutant of Rab11 (Rab11S25N). This tubularized compartment was not accessible to Tf internalized at temperatures <20 degrees C, suggesting that it is of recycling endosomal origin. Overexpression of Rab11wt, Rab11Q70L, and Rab11S25N also inhibited STxB and TGN38 transport from endosomes to the TGN. These results suggest that Rab11 influences endosome to TGN trafficking primarily by regulating membrane distribution inside the early endosomal pathway.
- Published
- 2000
- Full Text
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8. Tight junction, a platform for trafficking and signaling protein complexes.
- Author
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Zahraoui A, Louvard D, and Galli T
- Subjects
- Membrane Proteins metabolism, SNARE Proteins, Protein Transport physiology, Signal Transduction physiology, Tight Junctions metabolism, Vesicular Transport Proteins
- Published
- 2000
- Full Text
- View/download PDF
9. Role of tetanus neurotoxin insensitive vesicle-associated membrane protein (TI-VAMP) in vesicular transport mediating neurite outgrowth.
- Author
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Martinez-Arca S, Alberts P, Zahraoui A, Louvard D, and Galli T
- Subjects
- Animals, Biological Transport drug effects, Botulinum Toxins pharmacology, Cell Differentiation, Exocytosis drug effects, Metalloendopeptidases pharmacology, Nerve Tissue Proteins metabolism, PC12 Cells, Protein Binding, R-SNARE Proteins, Rats, SNARE Proteins, Staurosporine pharmacology, Synaptosomal-Associated Protein 25, Tetanus Toxin pharmacology, Intracellular Membranes metabolism, Membrane Proteins metabolism, Neurites, Neurons cytology, Vesicular Transport Proteins
- Abstract
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 NH(2)-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 NH(2)-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 NH(2)-terminal domain as a key regulator in this process.
- Published
- 2000
- Full Text
- View/download PDF
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