How Calcium Affects Bestrophins
Author Information
Author(s): Kranjc Agata, Grillo Federico W., Rievaj Juraj, Boccaccio Anna, Pietrucci Fabio, Menini Anna, Carloni Paolo, Anselmi Claudio
Primary Institution: International School for Advanced Studies (SISSA/ISAS), Trieste, Italy
Hypothesis
The Asp-rich domain of bestrophins is involved in Ca2+ binding and activation.
Conclusion
The study confirms that mutations in the Asp-rich domain of bestrophins significantly affect their function and Ca2+-activated Cl− currents.
Supporting Evidence
- Molecular dynamics simulations identified key residues in the Asp-rich domain that bind Ca2+.
- Electrophysiological experiments confirmed that mutations in the Asp-rich domain affect Ca2+-activated Cl− currents.
- The study suggests that at least two Ca2+-binding sites are present in the Asp-rich domain.
Takeaway
Bestrophins are proteins that help control chloride ions in cells, and this study shows how calcium affects their function by binding to specific parts of the protein.
Methodology
The study used molecular dynamics simulations and electrophysiological experiments to analyze the effects of mutations in the Asp-rich domain of bestrophins.
Limitations
The lack of structural information about the transmembrane region of the channel limits the understanding of how Ca2+ binding affects channel gating.
Statistical Information
P-Value
p<0.002
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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