ArticleThe Journal of cell biology1995
Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 126 citations in OpenAlex.
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- Epileptic Phenotypes Associated With SNAREs and Related Synaptic Vesicle Exocytosis Machinery.Frontiers in neurology · 2021Review
- Ablation of All Synaptobrevin vSNAREs Blocks Evoked But Not Spontaneous Neurotransmitter Release at Neuromuscular Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Astrocyte VAMP3 vesicles undergo Ca2+ -independent cycling and modulate glutamate transporter trafficking.The Journal of physiology · 2015Article
- All three components of the neuronal SNARE complex contribute to secretory vesicle docking.The Journal of cell biology · 2012Article
- Sunday driver interacts with two distinct classes of axonal organelles.The Journal of biological chemistry · 2009Article
- A role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex dimerization during neurosecretion.Molecular biology of the cell · 2008Article
- Lysosomes are the major vesicular compartment undergoing Ca2+-regulated exocytosis from cortical astrocytes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Membrane fusion by VAMP3 and plasma membrane t-SNAREs.Experimental cell research · 2007Article
- Detecting fluorescent protein expression and co-localisation on single secretory vesicles with linear spectral unmixing.European biophysics journal : EBJ · 2006Article
- Synaptobrevin2-expressing vesicles in rat astrocytes: insights into molecular characterization, dynamics and exocytosis.The Journal of physiology · 2006Article
- v-SNAREs control exocytosis of vesicles from priming to fusion.The EMBO journal · 2005Article
- EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.Molecular biology of the cell · 2005Article
- Cross talk between tetanus neurotoxin-insensitive vesicle-associated membrane protein-mediated transport and L1-mediated adhesion.Molecular biology of the cell · 2003Article
- Reversible suppression of glutamatergic neurotransmission of cerebellar granule cells in vivo by genetically manipulated expression of tetanus neurotoxin light chain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Targeted trafficking of neurotransmitter receptors to synaptic sites.Molecular neurobiology · 2002Review
- A ganglioside-specific sialyltransferase localizes to axons and non-Golgi structures in neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and Is required for late endosome-lysosome fusion.Molecular biology of the cell · 2000Article
- Role of plasma membrane transporters in muscle metabolism.The Biochemical journal · 2000Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
There is strong evidence to indicate that proteins of the synaptobrevin family play a key role in exocytosis. Synaptobrevin 1 and 2 are expressed at high concentration in brain where they are localized on synaptic vesicles. Cellubrevin, a very similar protein, has a widespread tissue distribution and in fibroblasts is localized on endosome-derived, transferin receptor-positive vesicles. Since brain cellubrevin is not detectable in synaptic vesicles, we investigated whether cellubrevin and the synaptobrevins are differentially targeted when co-expressed in the same cell. We report that in the nervous system cellubrevin is expressed at significant levels only by glia and vascular cells. However, cellubrevin is coexpressed with the two synaptobrevins in PC12 cells, a neuroendocrine cell line which contains synaptic vesicle-like microvesicles. In PC12 cells, cellubrevin has a distribution very similar to that of synaptobrevin 1 and 2. The three proteins are targeted to neurites which exclude the transferrin receptor and are enriched in synaptic-like microvesicles and dense-core granules. They are recovered in the synaptic-like microvesicle peak of glycerol velocity gradients, have a similar distribution in isopycnic fractionation and are coprecipitated by anti-synaptobrevin 2 immunobeads. Finally, cellubrevin, like the synaptobrevins, interact with the neuronal t-SNAREs syntaxin 1 and SNAP-25. These results suggest that cellubrevin and the synaptobrevins have similar function and do not play a specialized role in constitutive and regulated exocytosis, respectively.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.