ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008
Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Disease-causing mutations in Synaptotagmin can act via dominant-negative, gain-of-function or haploinsufficient mechanisms.bioRxiv : the preprint server for biology · 2026Article
- Pharmaceutical agent cetylpyridinium chloride inhibits immune mast cell function by interfering with calcium mobilization.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2023Article
- Physiologic and Nanoscale Distinctions Define Glutamatergic Synapses in Tonic vs Phasic Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Expanding the genotype and phenotype spectrum of SYT1-associated neurodevelopmental disorder.Genetics in medicine : official journal of the American College of Medical Genetics · 2022Article
- Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021Review
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- The C2A domain of synaptotagmin is an essential component of the calcium sensor for synaptic transmission.PloS one · 2020Article
- Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Different states of synaptotagmin regulate evoked versus spontaneous release.Nature communications · 2016Article
- The structure and function of 'active zone material' at synapses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.Biophysical journal · 2015Article
- The synaptotagmin juxtamembrane domain is involved in neuroexocytosis.FEBS open bio · 2015Article
- Calcium sensitive ring-like oligomers formed by synaptotagmin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Conformational dynamics of calcium-triggered activation of fusion by synaptotagmin.Biophysical journal · 2013Article
- Genetic analysis of synaptotagmin C2 domain specificity in regulating spontaneous and evoked neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Detection of highly curved membrane surfaces using a cyclic peptide derived from synaptotagmin-I.ACS chemical biology · 2012Article
- Mechanism for calcium ion sensing by the C2A domain of synaptotagmin I.Biophysical journal · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptotagmin I is the Ca(2+) sensor for fast, synchronous release of neurotransmitter; however, the molecular interactions that couple Ca(2+) binding to membrane fusion remain unclear. The structure of synaptotagmin is dominated by two C(2) domains that interact with negatively charged membranes after binding Ca(2+). In vitro work has implicated a conserved basic residue at the tip of loop 3 of the Ca(2+)-binding pocket in both C(2) domains in coordinating this electrostatic interaction with anionic membranes. Although results from cultured cells suggest that the basic residue of the C(2)A domain is functionally significant, such studies provide contradictory results regarding the importance of the C(2)B basic residue during vesicle fusion. To directly test the functional significance of each of these residues at an intact synapse in vivo, we neutralized either the C(2)A or the C(2)B basic residue and assessed synaptic transmission at the Drosophila neuromuscular junction. The conserved basic residues at the tip of the Ca(2+)-binding pocket of both the C(2)A and C(2)B domains mediate Ca(2+)-dependent interactions with anionic membranes and are required for efficient evoked transmitter release. Our results directly support the hypothesis that the interactions between synaptotagmin and the presynaptic membrane, which are mediated by the basic residues at the tip of both the C(2)A and C(2)B Ca(2+)-binding pockets, are critical for coupling Ca(2+) influx with vesicle fusion during synaptic transmission in vivo. Our model for synaptotagmin's direct role in coupling Ca(2+) binding to vesicle fusion incorporates this finding with results from multiple in vitro and in vivo studies.
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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.