ArticleThe Journal of biological chemistry2011
Crystal structure of the cytoplasmic phosphatase and tensin homolog (PTEN)-like region of Ciona intestinalis voltage-sensing phosphatase provides insight into substrate specificity and redox regulation of the phosphoinositide phosphatase activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 49 citations in OpenAlex.
- Elucidating PTEN conformational dynamics and phosphatase regulation via integrative modeling and mutation prediction.Structure (London, England : 1993) · 2025Article
- Nonsubstrate PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Voltage sensors.Molecular pharmacology · 2025Review
- Predicting the Structural Impact of Human Alternative Splicing.bioRxiv : the preprint server for biology · 2023Article
- Role of K364 next to the active site cysteine in voltage-dependent phosphatase activity of Ci-VSP.Biophysical journal · 2023Article
- Voltage-sensing phosphatase (Vsp) regulates endocytosis-dependent nutrient absorption in chordate enterocytes.Communications biology · 2022Article
- 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
- The structural basis of PTEN regulation by multi-site phosphorylation.Nature structural & molecular biology · 2021Article
- Structural Mechanisms of PTEN Regulation.Cold Spring Harbor perspectives in medicine · 2020Review
- Dual-Specific Protein and Lipid Phosphatase PTEN and Its Biological Functions.Cold Spring Harbor perspectives in medicine · 2020Review
- Dynamic structural rearrangements and functional regulation of voltage-sensing phosphatase.The Journal of physiology · 2019Review
- Article
- A126 in the active site and TI167/168 in the TI loop are essential determinants of the substrate specificity of PTEN.Cellular and molecular life sciences : CMLS · 2018Article
- Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018Review
- 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
- Structural mechanisms of plant glucan phosphatases in starch metabolism.The FEBS journal · 2016Review
- 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
- Voltage-Gated Potassium Channels: A Structural Examination of Selectivity and Gating.Cold Spring Harbor perspectives in biology · 2016Review
- Allosteric substrate switching in a voltage-sensing lipid phosphatase.Nature chemical biology · 2016Article
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8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) has a transmembrane voltage sensor domain and a cytoplasmic region sharing similarity to the phosphatase and tensin homolog (PTEN). It dephosphorylates phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon membrane depolarization. The cytoplasmic region is composed of a phosphatase domain and a putative membrane interaction domain, C2. Here we determined the crystal structures of the Ci-VSP cytoplasmic region in three distinct constructs, wild-type (248-576), wild-type (236-576), and G365A mutant (248-576). The crystal structure of WT-236 and G365A-248 had the disulfide bond between the catalytic residue Cys-363 and the adjacent residue Cys-310. On the other hand, the disulfide bond was not present in the crystal structure of WT-248. These suggest the possibility that Ci-VSP is regulated by reactive oxygen species as found in PTEN. These structures also revealed that the conformation of the TI loop in the active site of the Ci-VSP cytoplasmic region was distinct from the corresponding region of PTEN; Ci-VSP has glutamic acid (Glu-411) in the TI loop, orienting toward the center of active site pocket. Mutation of Glu-411 led to acquirement of increased activity toward phosphatidylinositol 3,5-bisphosphate, suggesting that this site is required for determining substrate specificity. Our results provide the basic information of the enzymatic mechanism of Ci-VSP.
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