ArticleBiophysical journal2012
Coupling of Ci-VSP modules requires a combination of structure and electrostatics within the linker.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 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
- Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP.Nature communications · 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
- Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020Review
- 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
- Phosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependence.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
- Japanese encephalitis virus nonstructural protein NS5 interacts with mitochondrial trifunctional protein and impairs fatty acid β-oxidation.PLoS pathogens · 2015Article
- 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
- Voltage-sensing phosphatase modulation by a C2 domain.Frontiers in pharmacology · 2015Article
- Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research.Frontiers in pharmacology · 2015Review
- Phosphatase activity of the voltage-sensing phosphatase, VSP, shows graded dependence on the extent of activation of the voltage sensor.The Journal of physiology · 2014Article
- Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain.Nature structural & molecular biology · 2014Article
- The linker pivot in Ci-VSP: the key to unlock catalysis.PloS one · 2013Article
- PtdIns(4,5)P2-mediated cell signaling: emerging principles and PTEN as a paradigm for regulatory mechanism.Advances in experimental medicine and biology · 2013Review
- A human phospholipid phosphatase activated by a transmembrane control module.Journal of lipid research · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-sensitive phosphatase Ci-VSP consists of an intracellular phosphatase domain (PD) coupled to a transmembrane voltage-sensor domain (VSD). Depolarization triggers the selective dephosphorylation of phosphoinositides. However, the molecular mechanisms of coupling are still elusive. To clarify the role of the VSD-PD linker as a putative partner for electrostatic interactions with the membrane, we carried out a cysteine-scanning mutagenesis of the whole motif M240-K257. Upon coexpression with PI(4,5)P(2)-sensitive KCNQ2/KCNQ3 channels in Xenopus oocytes, we identified four positions (A242C, R245C, K252C, and Y255C) with a completely abrogated PD activity. Because the mutation effect occurred periodically, we hypothesize that α-helical elements exist within the linker, with a gap near position S249. The combination of these results with the analysis of transient sensing currents of the VSD revealed distinct roles for the N-terminal (M240-S249) and C-terminal (Q250-K257) linker motifs in the VSD-PD coupling. According to our functional results, the computational structure prediction of the Q239-D258 fragment confirmed α-helical structures within the linker, with a short β-turn around S249 in the activated conformation. Remarkably, the position K252 may be a candidate for interacting with the PD rather than for binding to the membrane. This provides the first insight (to our knowledge) into the direct intervention of the linker in the VSD-PD coupling process.
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