ArticleBiophysical journal2012
Mechanism for calcium ion sensing by the C2A domain of synaptotagmin I.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Intrinsically disordered proteins in synaptic vesicle trafficking and release.The Journal of biological chemistry · 2019Review
- Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR.Biophysical journal · 2018Article
- Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1.Molecular biology of the cell · 2016Article
- Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.Biophysical journal · 2015Article
- Randomly organized lipids and marginally stable proteins: a coupling of weak interactions to optimize membrane signaling.Biochimica et biophysica acta · 2014Article
- Alternate splicing of dysferlin C2A confers Ca²⁺-dependent and Ca²⁺-independent binding for membrane repair.Structure (London, England : 1993) · 2014Article
- Is it zippered? Does it flare? That darn complexin clamping SNARE.Biophysical journal · 2013Article
- Allostery and instability in the functional plasticity of synaptotagmin I.Communicative & integrative biology · 2013Article
- Negative coupling as a mechanism for signal propagation between C2 domains of synaptotagmin I.PloS one · 2012Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C2A domain is one of two calcium ion (Ca(2+))- and membrane-binding domains within synaptotagmin I (Syt I), the identified Ca(2+) sensor for regulated exocytosis of neurotransmitter. We propose that the mechanistic basis for C2A's response to Ca(2+) and cellular function stems from marginal stability and ligand-induced redistributions of protein conformers. To test this hypothesis, we used a combination of calorimetric and fluorescence techniques. We measured free energies of stability by globally fitting differential scanning calorimetry and fluorescence lifetime spectroscopy denaturation data, and found that C2A is weakly stable. Additionally, using partition functions in a fluorescence resonance energy transfer approach, we found that the Ca(2+)- and membrane-binding sites of C2A exhibit weak cooperative linkage. Lastly, a dye-release assay revealed that the Ca(2+)- and membrane-bound conformer subset of C2A promote membrane disruption. We discuss how these phenomena may lead to both cooperative and functional responses of Syt I.
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