Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The second PI(3,5)P2 binding site in the S0 helix of KCNQ1 stabilizes PIP2-at the primary PI1 site with potential consequences on intermediate-to-open state transition.

Biological chemistry - 28 Mar 2023

Dellin Maurice, Rohrbeck Ina, Asrani Purva, Schreiber Julian A, Ritter Nadine, Glorius Frank, Wünsch Bernhard, Budde Thomas, Temme Louisa, Strünker Timo, Stallmeyer Birgit, Tüttelmann Frank, Meuth Sven G, Spehr Marc, Matschke Johann, Steinbicker Andrea, Gatsogiannis Christos, Stoll Raphael, Strutz-Seebohm Nathalie, Seebohm Guiscard

Abstract excerpt

The Phosphatidylinositol 3-phosphate 5-kinase Type III PIKfyve is the main source for selectively generated phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2), a known regulator of membrane protein trafficking. PI(3,5)P2 facilitates the cardiac KCNQ1/KCNE1 channel plasma membrane abundance and therewith increases the macroscopic current amplitude. Functional-physical interaction of PI(3,5)P2 with membrane proteins...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Membrane

Share to KCNQ1 Potassium Channel

Share to Mutation

Share to Phosphatidylinositol 4,5-Diphosphate

Source

Identifiers

PMID: 36809224
DOI: 10.1515/hsz-2022-0247

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The second PI(3,5)P2 binding site in the S0 helix of KCNQ1 stabilizes PIP2-at the primary PI1 site with potential consequences on intermediate-to-open state transition.PMID 36809224Read ↗

Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gatingSemantic proximity Read ↗

Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome.Semantic proximity Read ↗

KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP2) sensitivity of IKs to modulate channel activity.Semantic proximity Read ↗

Migration of PIP2 lipids on voltage-gated potassium channel surface influences channel deactivation.Semantic proximity Read ↗

PIP <sub>2</sub> stabilizes Na <sub>V</sub> 1.5 gating and links receptor signaling to cardiac late sodium currentSemantic proximity Read ↗

PIP <sub>2</sub> -dependent coupling of voltage sensor and pore domains in K <sub>v</sub> 7.2Semantic proximity Read ↗

A dual polybasic motif determines phosphoinositide binding and regulation in the P2X channel family.Semantic proximity Read ↗

Structural determinants of phosphatidylinositol 4,5-bisphosphate (PIP2) regulation of BK channel activity through the RCK1 Ca2+ coordination site.Semantic proximity Read ↗

Phosphatidylinositol-4,5-bisphosphate is required for KCNQ1/KCNE1 channel function but not anterograde trafficking.Semantic proximity Read ↗

Crystal structure of the mammalian GIRK2 K+ channel and gating regulation by G proteins, PIP2, and sodium.Semantic proximity Read ↗

Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of the Kir2.1-Regulated Inward Rectifier Potassium Currents.Semantic proximity Read ↗

Distant cytosolic residues mediate a two-way molecular switch that controls the modulation of inwardly rectifying potassium (Kir) channels by cholesterol and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.