Tetanus neurotoxin-insensitive vesicle-associated membrane protein localizes to a presynaptic membrane compartment in selected terminal subsets of the rat brain

Muzerelle, Aude; Alberts, Pēteris; Martinez-Arca, Sonia; Jeannequin, Odile; Lafaye, Pierre; Mazié, J. C.; Galli, Thierry; Gaspar, Patricia

doi:10.1016/s0306-4522(03)00567-0

Cited by 46 publications

(41 citation statements)

References 53 publications

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“…Because TI-VAMP is not expressed at Schaffer collateral terminals onto rat CA1 pyramidal cells (ref. 9; Fig. 5a), we anticipated this form of exocytosis may not be observed at these synapses.…”

Section: Asynchronous Release Evoked At Mossy Fiber (Mf) Terminals Ismentioning

confidence: 88%

“…mocha and control (heterozygous littermates) 1-to 2-month-old mice were anesthetized with 35% chloral hydrate or pentobarbital and perfused through the heart with 4% paraformaldehyde. The dissected brains were fixed overnight in 4% paraformaldehyde in PBS, cut on a vibratome into 30-m-thick sections, and processed for immunofluorescence as described (9). Confocal laser-scanning microscopy was performed by using an SP2 confocal microscope (Leica Microsystems, Mannheim, Germany).…”

Section: Methodsmentioning

confidence: 99%

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Loss of AP-3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses

Scheuber

Rudge

Danglot

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

120

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Synaptic vesicle (SV) exocytosis mediating neurotransmitter release occurs spontaneously at low intraterminal calcium concentrations and is stimulated by a rise in intracellular calcium. Exocytosis is compensated for by the reformation of vesicles at plasma membrane and endosomes. Although the adaptor complex AP-3 was proposed to be involved in the formation of SVs from endosomes, whether its function has an indirect effect on exocytosis remains unknown. Using mocha mice, which are deficient in functional AP-3, we identify an AP-3-dependent tetanus neurotoxin-resistant asynchronous release that can be evoked at hippocampal mossy fiber (MF) synapses. Presynaptic targeting of the tetanus neurotoxin-resistant vesicle soluble N -ethylmaleimide-sensitive factor attachment protein receptor (SNARE) tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) is lost in mocha hippocampal MF terminals, whereas the localization of synaptobrevin 2 is unaffected. In addition, quantal release in mocha cultures is more frequent and more sensitive to sucrose. We conclude that lack of AP-3 results in more constitutive secretion and loss of an asynchronous evoked release component, suggesting an important function of AP-3 in regulating SV exocytosis at MF terminals.

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Section: Asynchronous Release Evoked At Mossy Fiber (Mf) Terminals Ismentioning

confidence: 88%

Section: Methodsmentioning

confidence: 99%

Loss of AP-3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses

Scheuber

Rudge

Danglot

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

120

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“…Synaptic vesicles are enriched in nerve terminals, where they are continuously regenerated by membrane recycling, whereas lysosomes are selectively localized in cell bodies and dendrites and are excluded from axons and axon terminals. However, it has been shown that neuron-specific AP-3 subunits are present in axons (Seong et al, 2005) and that some membrane proteins such as TI-VAMP/VAMP7, the vacuolar proton pump, ClC3, Cln3, and the Niemann-Pick type C1 protein are present both on lysosomes and on subpopulations of axonal vesicles (Luiro et al, 2001;Stobrawa et al, 2001;Li et al, 2002;Karten et al, 2003;Muzerelle et al, 2003;Kyttala et al, 2004a,b). Interestingly, TI-VAMP/VAMP7 and Cln3 have been reported to be trafficked by AP-3-dependent mechanisms Kyttala et al, 2004b).…”

Section: Discussionmentioning

confidence: 99%

“…Consistent with the presence of ubiquitous AP-3 complexes containing the ␤3A subunit, ϳ17% of the proteins identified could be assigned to the category of lysosomes/lysosome-related organelles, which included AP-3 cargoes (LAMP1 and LAMP2) and BLOC-I complex subunits (Figure 2 and Supplemental Table 1). Some proteins, such as vacuolar proton pump subunits and vesicleassociated membrane protein (VAMP)7/TI-VAMP are present both in synaptic vesicles (synaptic vesicle subpopulations in the case of VAMP7/TI-VAMP) and lysosomes (Advani et al, 1999;Martinez-Arca et al, 2003;Muzerelle et al, 2003). Interestingly, VAMP7-TI-VAMP was shown to be sorted by AP-3-dependent mechanisms .…”

mentioning

confidence: 99%

Phosphatidylinositol-4-Kinase Type II α Is a Component of Adaptor Protein-3-derived Vesicles

Salazar

Craige

Wainer

et al. 2005

MBoC

101

136

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A membrane fraction enriched in vesicles containing the adaptor protein (AP) -3 cargo zinc transporter 3 was generated from PC12 cells and was used to identify new components of these organelles by mass spectrometry. Proteins prominently represented in the fraction included AP-3 subunits, synaptic vesicle proteins, and lysosomal proteins known to be sorted in an AP-3-dependent way or to interact genetically with AP-3. A protein enriched in this fraction was phosphatidylinositol-4-kinase type II␣ (PI4KII␣). Biochemical, pharmacological, and morphological analyses supported the presence of PI4KII␣ in AP-3-positive organelles. Furthermore, the subcellular localization of PI4KII␣ was altered in cells from AP-3-deficient mocha mutant mice. The PI4KII␣ normally present both in perinuclear and peripheral organelles was substantially decreased in the peripheral membranes of AP-3-deficient mocha fibroblasts. In addition, as is the case for other proteins sorted in an AP-3-dependent way, PI4KII␣ content was strongly reduced in nerve terminals of mocha hippocampal mossy fibers. The functional relationship between AP-3 and PI4KII␣ was further explored by PI4KII␣ knockdown experiments. Reduction of the cellular content of PI4KII␣ strongly decreased the punctate distribution of AP-3 observed in PC12 cells. These results indicate that PI4KII␣ is present on AP-3 organelles where it regulates AP-3 function. INTRODUCTIONMembrane-enclosed organelles possess distinctive protein compositions that are dynamically maintained by inbound and outbound vesicle carriers. These vesicles selectively concentrate appropriate membrane proteins while leaving behind resident proteins found in the donor organelle, a process called sorting (Bonifacino and Glick, 2004). Central to membrane protein sorting and vesiculation are a family of cytosolic coat complexes that mediate vesicle budding and function as cargo-specific adaptors. These include monomeric proteins and the heterotetrameric adaptor proteins (AP)-1, -2, -3, and -4 (Bonifacino and Glick, 2004;Robinson, 2004). These coats participate in the generation of vesicles that carry a unique array of membrane protein "cargoes." The characterization of these carriers has played a major role in the functional dissection of coat-dependent sorting and vesiculation mechanisms. For example, vesicles "in a basket" isolated from brain led to the biochemical identification of the first sorting machinery, clathrin and the AP-1 and AP-2 adaptors (Kanaseki and Kadota, 1969;Pearse, 1975;Pfeffer and Kelly, 1981;Pearse and Crowther, 1987). Subsequent studies of cargo molecules in brain clathrin-coated vesicles were crucial in revealing mechanisms of synaptic vesicle recycling (Pfeffer and Kelly, 1985;Maycox et al., 1992;Blondeau et al., 2004). The advent of complete genome sequencing and the concomitant development of informatics tools has led to the rapid identification of proteins by mass spectrometry (Taylor et al., 2003). Application of these methodologies to clathrin-coated vesicles has allowed the identifi...

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“…3 Pioneering work on VAMP7 knock down and over-expression of its regulatory aminoterminal Longin domain have underlined its importance in several cellular processes in different cell types. VAMP7 dependent trafficking was shown to participate in apical polarity, 4 neurite growth, 5 cell adhesion, 6 transport to lysosome from both early endosomes and TGN, [7][8][9] cell migration, exosome and lysosomal secretion, 10,11 and autophagy. 12, 13 We previously showed the involvement of VAMP7 in polarized apical transport 4,14 and its occurrence in detergent resistant membranes.…”

Section: Introductionmentioning

confidence: 99%

Role of tetanus neurotoxin insensitive vesicle-associated membrane protein in membrane domains transport and homeostasis

et al. 2015

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Keywords: exocytosis, Golgi apparatus, SNARE, sphingolipids, TI-VAMP/VAMP7 Abbreviations: BFA, Brefeldin A; Cer, Ceramide; ER, Endoplasmic Reticulum; GlcCer, Glucosylceramide; GM3, ganglioside monosialic acid 3; GPI, Glycosylphosphatidylinositol; GSL, Glycosphingolipids; LC, Long Chain; PI, Phosphatidylinositide; PM, Plasma Membrane; SM, Sphingomyelin; TGN, D Trans-Golgi Network; TI-VAMP/VAMP7, Tetanus neurotoxin-insensitive vesicle-associated membrane protein / Vesicle associated membrane protein 7; VLC, very long vhain; VSVG, Vesicular Stomatitis Virus GlycoproteinBiological membranes in eukaryotes contain a large variety of proteins and lipids often distributed in domains in plasma membrane and endomembranes. Molecular mechanisms responsible for the transport and the organization of these membrane domains along the secretory pathway still remain elusive. Here we show that vesicular SNARE TI-VAMP/VAMP7 plays a major role in membrane domains composition and transport. We found that the transport of exogenous and endogenous GPI-anchored proteins was altered in fibroblasts isolated from VAMP7-knockout mice. Furthermore, disassembly and reformation of the Golgi apparatus induced by Brefeldin A treatment and washout were impaired in VAMP7-depleted cells, suggesting that loss of VAMP7 expression alters biochemical properties and dynamics of the Golgi apparatus. In addition, lipid profiles from these knockout cells indicated a defect in glycosphingolipids homeostasis. We conclude that VAMP7 is required for effective transport of GPI-anchored proteins to cell surface and that VAMP7-dependent transport contributes to both sphingolipids and Golgi homeostasis.

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Tetanus neurotoxin-insensitive vesicle-associated membrane protein localizes to a presynaptic membrane compartment in selected terminal subsets of the rat brain

Cited by 46 publications

References 53 publications

Loss of AP-3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses

Loss of AP-3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses

Phosphatidylinositol-4-Kinase Type II α Is a Component of Adaptor Protein-3-derived Vesicles

Role of tetanus neurotoxin insensitive vesicle-associated membrane protein in membrane domains transport and homeostasis

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