ArticleThe Journal of general physiology2009
Coupling between the voltage-sensing and phosphatase domains of Ci-VSP.
Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 66 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
- Hydrophobic residues in S1 modulate enzymatic function and voltage sensing in voltage-sensing phosphatase.The Journal of general physiology · 2024Article
- Effect of a sensing charge mutation on the deactivation of KV7.2 channels.The Journal of general physiology · 2024Article
- 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
- Modulation of KFrontiers in pharmacology · 2020Article
- Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020Review
- Dynamic structural rearrangements and functional regulation of voltage-sensing phosphatase.The Journal of physiology · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Article
- Dimerization of the voltage-sensing phosphatase controls its voltage-sensing and catalytic activity.The Journal of general physiology · 2018Article
- Hysteresis in voltage-gated channels.Channels (Austin, Tex.) · 2017Review
- Domain-to-domain coupling in voltage-sensing phosphatase.Biophysics and physicobiology · 2017Review
- Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Allosteric substrate switching in a voltage-sensing lipid phosphatase.Nature chemical biology · 2016Article
- Functional diversity of potassium channel voltage-sensing domains.Channels (Austin, Tex.) · 2016Review
- bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles.The Journal of general physiology · 2016Article
- Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research.Frontiers in pharmacology · 2015Review
- Ion channel regulation by phosphoinositides analyzed with VSPs-PI(4,5)P2 affinity, phosphoinositide selectivity, and PI(4,5)P2 pool accessibility.Frontiers in pharmacology · 2015Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP) shares high homology with the phosphatidylinositol phosphatase enzyme known as PTEN (phosphatase and tensin homologue deleted on chromosome 10). We have taken advantage of the similarity between these proteins to inquire about the coupling between the voltage sensing and the phosphatase domains in Ci-VSP. Recently, it was shown that four basic residues (R11, K13, R14, and R15) in PTEN are critical for its binding onto the membrane, required for its catalytic activity. Ci-VSP has three of the basic residues of PTEN. Here, we show that when R253 and R254 (which are the homologues of R14 and R15 in PTEN) are mutated to alanines in Ci-VSP, phosphatase activity is disrupted, as revealed by a lack of effect on the ionic currents of KCNQ2/3, where current decrease is a measure of phosphatase activity. The enzymatic activity was not rescued by the introduction of lysines, indicating that the binding is an arginine-specific interaction between the phosphatase binding domain and the membrane, presumably through the phosphate groups of the phospholipids. We also found that the kinetics and steady-state voltage dependence of the S4 segment movement are affected when the arginines are not present, indicating that the interaction of R253 and R254 with the membrane, required for the catalytic action of the phosphatase, restricts the movement of the voltage sensor.
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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.