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 Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking.

PloS one - 1 Jan 2015

Choveau Frank S, Zhang Jie, Bierbower Sonya M, Sharma Ramaswamy, Shapiro Mark S

Abstract excerpt

In the central and peripheral nervous system, the assembly of KCNQ3 with KCNQ2 as mostly heteromers, but also homomers, underlies "M-type" currents, a slowly-activating voltage-gated K+ current that plays a dominant role in neuronal excitability. KCNQ3 homomers yield much smaller currents compared to KCNQ2 or KCNQ4 homomers and KCNQ2/3 heteromers. This smaller current has been suggested to result either from...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to CHO Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetulus

Share to Endoplasmic Reticulum

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 26692086
DOI: 10.1371/journal.pone.0145367
PMCID: PMC4687061

Genes

KCNQ3
KCNQ2
KCNQ4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking.PMID 26692086Read ↗

Functional Interactions between KCNE1 C-Terminus and the KCNQ1 ChannelSemantic proximity Read ↗

Critical roles for the M3-S2 transduction linker domain in kainate receptor assembly and postassembly trafficking.Semantic proximity Read ↗

KCNQ2 and KCNQ5 form heteromeric channels independent of KCNQ3.Semantic proximity Read ↗

Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.Semantic proximity Read ↗

Calmodulin orchestrates the heteromeric assembly and the trafficking of KCNQ2/3 (Kv7.2/3) channels in neurons.Semantic proximity Read ↗

Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels.Semantic proximity Read ↗

Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in the KCNQ2 and KCNQ3 C-terminal domains.Semantic proximity Read ↗

Pore determinants of KCNQ3 K+ current expression.Semantic proximity Read ↗

Role of an S4-S5 linker lysine in the trafficking of the Ca(2+)-activated K(+) channels IK1 and SK3.Semantic proximity Read ↗

Atypical gating of M-type potassium channels conferred by mutations in uncharged residues in the S4 region of KCNQ2 causing benign familial neonatal convulsions.Semantic proximity Read ↗

Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity.Semantic proximity Read ↗

Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1.Semantic proximity Read ↗

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