ArticleMolecular biology of the cell2008
A role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex dimerization during neurosecretion.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Article
- Review
- Botulinum Toxin A and Lower Urinary Tract Dysfunction: Pathophysiology and Mechanisms of Action.Toxins · 2016Review
- Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion.The Journal of biological chemistry · 2015Article
- Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Two synaptobrevin molecules are sufficient for vesicle fusion in central nervous system synapses.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- SNARE motif-mediated sorting of synaptobrevin by the endocytic adaptors clathrin assembly lymphoid myeloid leukemia (CALM) and AP180 at synapses.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Calcium-dependent regulation of SNARE-mediated membrane fusion by calmodulin.The Journal of biological chemistry · 2010Article
- Combined kinase inhibition modulates parkin inactivation.Human molecular genetics · 2009Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE complexes are in apposition, and it involves residues from the vesicle-associated SNARE synaptobrevin 2 that lie close to the cytosol-membrane interface within the full-length protein. Mutation of these residues reduces stability of dimers formed between SNARE complexes, without affecting the stability of each individual SNARE complex. These mutations also cause a corresponding decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells. Moreover, such synaptobrevin 2 mutants give rise to a dominant-negative inhibition of exocytosis. These data are consistent with an important role for SNARE complex dimers in neurosecretion.
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Registered trials
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