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Improved detection of electrical activity with a voltage probe based on a voltage‐sensing phosphatase
An improved voltage probe named Mermaid2 is developed that provides ratiometric readouts of electrical activity with fast kinetics and great sensitivity, and was able to detect single‐event electrical activity both in vitro and in vivo.
Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid
- Souhei Sakata, Yuka Jinno, Akira Kawanabe, Y. Okamura
- Biology, ChemistryProceedings of the National Academy of Sciences
- 21 June 2016
Results indicate that the voltage sensor regulates Ci-VSP catalytic activity by causing conformational changes in the entire catalytic region, without changing their distance from the plasma membrane.
A diffraction-quality protein crystal processed as an autophagic cargo.
Functional diversity of voltage‐sensing phosphatases in two urodele amphibians
Both VSPs showed “sensing” currents, indicating that their voltage sensor domains are functional, and the phosphatase activity of Cp‐VSP was found to be voltage dependent, as shown by its ability to regulate the conductance of coexpressed GIRK2 channels, but Hn‐V SP lacked such phosphat enzyme activity due to the truncation of its C2 domain.
Comparison between mouse and sea urchin orthologs of voltage-gated proton channel suggests role of S3 segment in activation gating.
Optically detected structural change in the N-terminal region of the voltage-sensor domain.
Are cerebrovascular factors involved in Alzheimer’s disease?
Genetically encoded bioluminescent voltage indicator for multi-purpose use in wide range of bioimaging
The first genetically encoded bioluminescent indicator for membrane voltage called LOTUS-V is developed, which extends the scope of excitable cell control and simultaneous voltage phenotyping, which should enable applications in bioscience, medicine and pharmacology previously not possible.
Rapid evaluation of a protein-based voltage probe using a field-induced membrane potential change.
The hydrophobic nature of a novel membrane interface regulates the enzyme activity of a voltage-sensing phosphatase
A membrane interface is reported (named ‘the hydrophobic spine’), which is essential for the coupling of the VSD and CCR and indicates that the voltage-dependent phosphatase activity of Ci-VSP depends on the hydrophobicity and presence of an aromatic ring in the hydrophic spine.