ArticleProceedings of the National Academy of Sciences of the United States of America2016
Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Nonsubstrate PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Coupling sensor to enzyme in the voltage sensing phosphatase.Nature communications · 2024Article
- Fluorescent Probes and Quenchers in Studies of Protein Folding and Protein-Lipid Interactions.Chemical record (New York, N.Y.) · 2024Review
- Interaction between S4 and the phosphatase domain mediates electrochemical coupling in voltage-sensing phosphatase (VSP).Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022Review
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- A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids.Heliyon · 2020Article
- Fluorescent amino acids as versatile building blocks for chemical biology.Nature reviews. Chemistry · 2020Review
- The contribution of voltage clamp fluorometry to the understanding of channel and transporter mechanisms.The Journal of general physiology · 2019Review
- Detection of NaBiophysical journal · 2019Article
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- Reinterpretation of the substrate specificity of the voltage-sensing phosphatase during dimerization.The Journal of general physiology · 2019Article
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Dynamic structural rearrangements and functional regulation of voltage-sensing phosphatase.The Journal of physiology · 2019Review
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- The Role of Proton Transport in Gating Current in a Voltage Gated Ion Channel, as Shown by Quantum Calculations.Sensors (Basel, Switzerland) · 2018Article
- Article
- Dynamic rearrangement of the intrinsic ligand regulates KCNH potassium channels.The Journal of general physiology · 2018Article
- Thermodynamics of voltage-gated ion channels.Biophysics reports · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoplasmic region of voltage-sensing phosphatase (VSP) derives the voltage dependence of its catalytic activity from coupling to a voltage sensor homologous to that of voltage-gated ion channels. To assess the conformational changes in the cytoplasmic region upon activation of the voltage sensor, we genetically incorporated a fluorescent unnatural amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), into the catalytic region of Ciona intestinalis VSP (Ci-VSP). Measurements of Anap fluorescence under voltage clamp in Xenopus oocytes revealed that the catalytic region assumes distinct conformations dependent on the degree of voltage-sensor activation. FRET analysis showed that the catalytic region remains situated beneath the plasma membrane, irrespective of the voltage level. Moreover, Anap fluorescence from a membrane-facing loop in the C2 domain showed a pattern reflecting substrate turnover. These 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.
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Registered trials
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.