ArticlePloS one2012
Negative coupling as a mechanism for signal propagation between C2 domains of synaptotagmin I.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR.Biophysical journal · 2018Article
- Oxidation increases the strength of the methionine-aromatic interaction.Nature chemical biology · 2016Article
- 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
- Copper binding affinity of the C2B domain of synaptotagmin-1 and its potential role in the nonclassical secretion of acidic fibroblast growth factor.Biochimica et biophysica acta · 2014Article
- Randomly organized lipids and marginally stable proteins: a coupling of weak interactions to optimize membrane signaling.Biochimica et biophysica acta · 2014Article
- Allostery and instability in the functional plasticity of synaptotagmin I.Communicative & integrative biology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synaptotagmin I (Syt I) is a vesicle-localized protein implicated in sensing the calcium influx that triggers fast synchronous release of neurotransmitter. How Syt I utilizes its two C2 domains to integrate signals and mediate neurotransmission has continued to be a controversial area of research, though prevalent hypotheses favor independent function. Using differential scanning calorimetry and fluorescence lifetime spectroscopy in a thermodynamic denaturation approach, we tested an alternative hypothesis in which both domains interact to cooperatively disseminate binding information. The free energy of stability was determined for C2A, C2B, and C2AB constructs by globally fitting both methods to a two-state model of unfolding. By comparing the additive free energies of C2A and C2B with C2AB, we identified a negative coupling interaction between the C2 domains of Syt I. This interaction not only provides a mechanistic means for propagating signals, but also a possible means for coordinating the molecular events of neurotransmission.
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Registered trials
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