ArticleProceedings of the National Academy of Sciences of the United States of America2004
Ca2+/calmodulin transfers the membrane-proximal lipid-binding domain of the v-SNARE synaptobrevin from cis to trans bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 48 citations in OpenAlex.
- The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021Review
- Characterization of P4 ATPase Phospholipid Translocases (Flippases) in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING INHIBITS INSULIN SECRETION.The Journal of biological chemistry · 2015Article
- Characterization of phospholipids in insulin secretory granules and mitochondria in pancreatic beta cells and their changes with glucose stimulation.The Journal of biological chemistry · 2015Article
- Coarse-grain simulations reveal movement of the synaptobrevin C-terminus in response to piconewton forces.Biophysical journal · 2012Article
- Massive calcium-activated endocytosis without involvement of classical endocytic proteins.The Journal of general physiology · 2011Article
- Calcium-dependent regulation of SNARE-mediated membrane fusion by calmodulin.The Journal of biological chemistry · 2010Article
- Evidence that electrostatic interactions between vesicle-associated membrane protein 2 and acidic phospholipids may modulate the fusion of transport vesicles with the plasma membrane.Molecular biology of the cell · 2009Article
- Sphingosine facilitates SNARE complex assembly and activates synaptic vesicle exocytosis.Neuron · 2009Article
- The structural and functional implications of linked SNARE motifs in SNAP25.Molecular biology of the cell · 2008Article
- Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking.The Journal of cell biology · 2008Article
- A role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex dimerization during neurosecretion.Molecular biology of the cell · 2008Article
- BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM.Plant cell reports · 2008Article
- Determinants of synaptobrevin regulation in membranes.Molecular biology of the cell · 2007Article
- A null mutation in VAMP1/synaptobrevin is associated with neurological defects and prewean mortality in the lethal-wasting mouse mutant.Neurogenetics · 2007Article
- Synaptic vesicle chips to assay botulinum neurotoxins.The Biochemical journal · 2005Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) protein interactions at the synaptic vesicle/plasma membrane interface play an essential role in neurotransmitter release. The membrane-proximal region (amino acids 77-90) of the v-SNARE vesicle-associated membrane protein 2 (VAMP 2, synaptobrevin) binds acidic phospholipids or Ca(2+)/calmodulin in a mutually exclusive manner, processes that are required for Ca(2+)-dependent exocytosis. To address the mechanisms involved, we asked whether this region of VAMP can interact with cis (outer vesicle leaflet) and/or trans (inner plasma membrane leaflet) lipids. To evaluate cis lipid binding, recombinant VAMP was reconstituted into liposomes and accessibility to site-directed antibodies was probed by surface plasmon resonance. Data indicated that the membrane-proximal domain of VAMP dips into the cis lipid bilayer, sequestering epitopes between the tetanus toxin cleavage site and the membrane anchor. These epitopes were unmasked by VAMP double mutation W89A, W90A, which abolishes lipid interactions. To evaluate trans lipid binding, VAMP was reconstituted in cis liposomes, which were then immobilized on beads. The ability of VAMP to capture protein-free (3)H-labeled trans liposomes was then measured. When cis lipid interactions were eliminated by omitting negatively charged lipids, trans lipid binding to VAMP was revealed. In contrast, when cis and trans liposomes both contained acidic headgroups (i.e., approximating physiological conditions), cis lipid interactions totally occluded trans lipid binding. In these conditions Ca(2+)/calmodulin displaced cis inhibition, transferring the lipid-binding domain of VAMP from the cis to the trans bilayer. Our results suggest that calmodulin acts as a unidirectional Ca(2+)-activated shuttle that docks the juxtamembrane portion of the v-SNARE in the target membrane to prepare fusion.
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