Document
type: Class

Continuant
type: Class

Virginia Commonwealth University, VCU
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

Entity
type: Class

Generically Dependent Continuant
type: Class

National Heart, Lung, and Blood Institute, NHLBI: R01HL059949
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

RDF description of PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker - http://orbis.uaslp.mx/vivo/individual/scopus3198
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date: 2026-08-24T21:53:06
publisher: vivo
type: Document

Proceedings of the National Academy of Sciences of the United States of America
type: Periodical
type: Journal
type: Collection
type: Thing
type: Document
type: Generically Dependent Continuant
type: Entity
publication venue for: PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker
type: Continuant
type: Information Content Entity

Article
type: Class

National Center for Research Resources, NCRR: S10RR027411
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker
most specific type: Document
most specific type: Article
chemicalscas: phosphatidylinositol 4,5 bisphosphate, 94161-15-6; Phosphatidylinositol 4,5-Diphosphate; Phospholipids; Potassium Channels, Voltage-Gated; Protein Subunits
type: Document
type: Entity
page end: E2408
has funding vehicle: National Institutes of Health, NIH
abstract: Voltage-gated K (Kv) channels couple the movement of a voltage sensor to the channel gate(s) via a helical intracellular region, the S4–S5 linker. A number of studies link voltage sensitivity to interactions of S4 charges with membrane phospholipids in the outer leaflet of the bilayer. Although the phospholipid phosphatidylinositol-4,5-bisphosphate (PIP2) in the inner membrane leaflet has emerged as a universal activator of ion channels, no such role has been established for mammalian Kv channels. Here we show that PIP2 depletion induced two kinetically distinct effects on Kv channels: an increase in voltage sensitivity and a concomitant decrease in current amplitude. These effects are reversible, exhibiting distinct molecular determinants and sensitivities to PIP2. Gating current measurements revealed that PIP2 constrains the movement of the sensor through interactions with the S4–S5 linker. Thus, PIP2 controls both the movement of the voltage sensor and the stability of the open pore through interactions with the linker that connects them. © 2012, National Academy of Sciences. All rights reserved.
accesstype: All Open Access, Bronze, Green
doi: 10.1073/pnas.1207901109
volume: 109
e iscopus: 2-s2.0-84866336468
related by: authorship_18598
type: Information Content Entity
related by: authorship_18600
type: Article
page start: E2399
has funding vehicle: National Center for Research Resources, NCRR: S10RR027411
related by: authorship_18601
abstract: Voltage-gated K%2b (Kv) channels couple the movement of a voltage sensor to the channel gate(s) via a helical intracellular region, the S4–S5 linker. A number of studies link voltage sensitivity to interactions of S4 charges with membrane phospholipids in the outer leaflet of the bilayer. Although the phospholipid phosphatidylinositol-4,5-bisphosphate (PIP2) in the inner membrane leaflet has emerged as a universal activator of ion channels, no such role has been established for mammalian Kv channels. Here we show that PIP2 depletion induced two kinetically distinct effects on Kv channels: an increase in voltage sensitivity and a concomitant decrease in current amplitude. These effects are reversible, exhibiting distinct molecular determinants and sensitivities to PIP2. Gating current measurements revealed that PIP2 constrains the movement of the sensor through interactions with the S4–S5 linker. Thus, PIP2 controls both the movement of the voltage sensor and the stability of the open pore through interactions with the linker that connects them. © 2012, National Academy of Sciences. All rights reserved.
related by: authorship_18599
type: Thing
issue: 36
related by: authorship_18602
pmid: 22891352
origen: scopus
related by: authorship_18603
type: Generically Dependent Continuant
has publication venue: Proceedings of the National Academy of Sciences of the United States of America
crisid: 3199
estado: published
date time value: article date 3199
type: Continuant
freetext keyword: Channel modulation; Lipids; Open probability; Voltage-gated channels phosphatidylinositol 4,5 bisphosphate; voltage gated potassium channel; phosphatidylinositol 4,5 bisphosphate; phospholipid; voltage gated potassium channel; animal cell; Article; channel gating; controlled study; ion conductance; lipid membrane; molecular interaction; nonhuman; priority journal; sensor; animal; article; channel gating; chemical structure; chemistry; kinetics; membrane potential; metabolism; molecular dynamics; mutagenesis; oocyte; patch clamp; physiology; protein subunit; X ray crystallography; Xenopus; Animals; Crystallography, X-Ray; Ion Channel Gating; Kinetics; Membrane Potentials; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis; Oocytes; Patch-Clamp Techniques; Phosphatidylinositol 4,5-Diphosphate; Phospholipids; Potassium Channels, Voltage-Gated; Protein Subunits; Xenopus
has funding vehicle: Virginia Commonwealth University, VCU
related by: authorship_18604
has funding vehicle: National Heart, Lung, and Blood Institute, NHLBI: R01HL059949

Information Content Entity
type: Class

National Institutes of Health, NIH
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker