Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes.

Cain, C C; Trimble, William S.; Lienhard, Gustav E.

doi:10.1016/s0021-9258(19)49748-2

Cited by 256 publications

(30 citation statements)

References 31 publications

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“…VAMP2 (also known as synaptobrevin-2) has been the first VAMP identified to be involved in GLUT4 translocation, as found in adipocytes, and has been mainly associated with insulin stimulation of GLUT4 exocytosis [62,63]. Also in muscle, VAMP2 has been shown to mediate insulin-stimulated GLUT4 exocytosis [64].…”

Section: Vamp2mentioning

confidence: 99%

Understanding the distinct subcellular trafficking of CD36 and GLUT4 during the development of myocardial insulin resistance

Luiken

Nabben

Neumann

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Section: Vamp2mentioning

confidence: 99%

Understanding the distinct subcellular trafficking of CD36 and GLUT4 during the development of myocardial insulin resistance

Luiken

Nabben

Neumann

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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“…Since homologues of synaptobrevin (Protopopov et al, 1993), syntaxin (Aalto et al, 1993), SNAP-25 (V. Bankaitis, personal communication), N-ethylmaleimide-sensitive fusion protein (NSF) (Wilson et al, 1989), and od/~-and 3,-SNAPs (Clary et al, 1990;Griff et al, 1992) are known to be involved in exocytosis from yeast, members of these protein families must participate in exocytosis from all cells. Accordingly, NSF and SNAPs (Whiteheart et al, 1993) are ubiquituously expressed and isoforms of synaptobrevin and syntaxins have been recently identified outside the nervous system (Cain et al, 1992;Chin et al, 1993;McMahon et al, 1993).…”

mentioning

confidence: 99%

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

Galli

Chilcote

Mundigl

et al. 1994

The Journal of Cell Biology

216

171

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Abstract. Cellubrevin is a member of the synaptobrevin/VAMP family of SNAREs, which has a broad tissue distribution. In fibroblastic cells it is concentrated in the vesicles which recycle transferrin receptors but its role in membrane trafficking and fusion remains to be demonstrated. Cellubrevin, like the synaptic vesicle proteins synaptobrevins I and 1I, can be cleaved by tetanus toxin, a metallo-endoprotease which blocks neurotransmitter release. However, nonneuronal cells are unaffected by the toxin due to lack of cell surface receptors for its heavy chain. To determine whether cellubrevin cleavage impairs exocytosis of recycling vesicles, we tested the effect of tetanus toxin light chain on the release of preinternalized transferrin from streptolysin-O-perforated CHO cells.The release was found to be temperature and ATP dependent as well as NEM sensitive. Addition of tetanus toxin light chain, but not of a proteolytically inactive form of the toxin, resulted in a partial inhibition of transferrin release which correlated with the toxinmediated cleavage of cellubrevin. The residual release of transferrin occurring after complete ceUubrevin degradation was still ATP dependent. Our results indicate that cellubrevin plays an important role in the constitutive exocytosis of vesicles which recycle plasmalemma receptors. The incomplete inhibition of transferrin release produced by the toxin suggests the existence of a cellubrevin-independent exocytotic mechanism, which may involve tetanus toxininsensitive proteins of the synaptobrevin/VAMP family.

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“…Isoforms of several other synaptic vesicle proteins have also been identified that are expressed in nonneuroendocrine cells (e.g., 7-10, 22, 24, 32, 45, 47, 58--60, 63, 71). For example, isoforms of the vSNARE synaptobrevin have been shown to colocalize with transferrincontaining recycling vesicles in fibroblasts (24, 47), with vesicles in the ER/Golgi region of skeletal muscle (58, 71), with zymogen granules of exocrine cells and dense core vesicles of J3 cells in pancreas (9, 59), with glucose transporter--containing vesicles in adipocytes(10), or water channels in the collecting ducts of kidney(22). Conversely, SCAMPs are not only constituents of secretory and endocytotic vesicles in nonneuroendocrine cells but also of synaptic vesicles(7,8,38).…”

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confidence: 99%

Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles.

Haass

Kartenbeck

Leube

1996

The Journal of Cell Biology

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Abstract. Certain properties of the highly specialized synaptic transmitter vesicles are shared by constitutively occurring vesicles. We and others have thus identified a cDNA in various nonneuroendocrine cell types of rat and human that is related to synaptophysin, one of the major synaptic vesicle membrane proteins, which we termed pantophysin. Here we characterize the gene structure, mRNA and protein expression, and intracellular distribution of pantophysin. Its mRNA is detected in murine cell types of nonneuroendocrine as well as of neuroendocrine origin. The intron/exon structure of the murine pantophysin gene is identical to that of synaptophysin except for the last intron that is absent in pantophysin. The encoded polypeptide of calculated mol wt 28,926 shares many sequence features with synaptophysin, most notably the four hydrophobic putative transmembrane domains, although the cytoplasmic end domains are completely different. Using antibodies against the unique carboxy terminus pantophysin can be detected by immunofluorescence microscopy in both exocrine and endocrine cells of human pancreas, and in cultured cells, colocalizing with constitutive secretory and endocytotic vesicle markers in nonneuroendocrine cells and with synaptophysin in cDNAtransfected epithelial cells. By immunoelectron microscopy, the majority of pantophysin reactivity is detected at vesicles with a diameter of <100 nm that have a smooth surface and an electron-translucent interior. Using cell fractionation in combination with immunoisolation, these vesicles are enriched in a light fraction and shown to contain the cellular vSNARE cellubrevin and the ubiquitous SCAMPs in epithelial cells and synaptophysin in neuroendocrine or cDNA-transfected nonneuroendocrine cells and neuroendocrine tissues. Pantophysin is therefore a broadly distributed marker of small cytoplasmic transport vesicles independent of their content. TRANSPORT between discontinuous cellular membranes is dependent on the presence of small carrier vesicles. Such vesicles have been identified and characterized in various pathways connecting, e.g., ERand Golgi apparatus, cis-and trans-Golgi cisternae, Golgi apparatus and lysosomes, trans-Golgi network and plasma membrane, or plasma membrane and endosomes (for description of such transport vesicles see references 4, 14, 28, 48, 51-53; for review see references 19, 56, 57). While it has been shown in many instances that the assembly of a defined "coat" is of importance for selective vesicle formation from a donor membrane (for example see references 2, 51, 55, 61, 65, 74), and that a multimolecular fusion complex is involved in vesicle fusion with a particular target membrane (for recent review see references 6, 20, 61, 66), very little is known about basic requirements for vesicle maintenance in the "free" cytoplasmic state. A suitable model system to examine principles determining vesicle morphogenesis is the synaptic, transmittercontaining, small secretory vesicle in neurons. Its major components have been characterized...

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Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes.

Cited by 256 publications

References 31 publications

Understanding the distinct subcellular trafficking of CD36 and GLUT4 during the development of myocardial insulin resistance

Understanding the distinct subcellular trafficking of CD36 and GLUT4 during the development of myocardial insulin resistance

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles.

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