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

Phosphorylation and protonation of neighboring MiRP2 sites: function and pathophysiology of MiRP2-Kv3.4 potassium channels in periodic paralysis.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Feb 2006

Abbott Geoffrey W, Butler Margaret H, Goldstein Steve A N

Abstract excerpt

MinK-related peptide 2 (MiRP2) and Kv3.4 subunits assemble in skeletal muscle to create subthreshold, voltage-gated potassium channels. MiRP2 acts on Kv3.4 to shift the voltage dependence of activation, speed recovery from inactivation, suppress cumulative inactivation and increase unitary conductance. We previously found an R83H missense mutation in MiRP2 that segregated with periodic paralysis in two families...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Paralyses, Familial Periodic

Share to Phosphorylation

Share to Potassium Channels, Voltage-Gated

Share to Protein Structure, Tertiary

Share to Protons

Source

Identifiers

PMID: 16449802
DOI: 10.1096/fj.05-5070com

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

Phosphorylation and protonation of neighboring MiRP2 sites: function and pathophysiology of MiRP2-Kv3.4 potassium channels in periodic paralysis.PMID 16449802Read ↗

MiRP2 Forms Potassium Channels in Skeletal Muscle with Kv3.4 and Is Associated with Periodic ParalysisSemantic proximity Read ↗

A Mixed Periodic Paralysis & Myotonia Mutant, P1158S, Imparts pH Sensitivity in Skeletal Muscle Voltage-gated Sodium ChannelsSemantic proximity Read ↗

NaV1.4 DI-S4 periodic paralysis mutation R222W enhances inactivation and promotes leak current to attenuate action potentials and depolarize muscle fibers.Semantic proximity Read ↗

A Mixed Periodic Paralysis & Myotonia Mutant, P1158S, Imparts pH-Sensitivity in Skeletal Muscle Voltage-gated Sodium Channels.Semantic proximity Read ↗

Disease‐associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanismSemantic proximity Read ↗

Genotype-phenotype correlation and therapeutic rationale in hyperkalemic periodic paralysis.Semantic proximity Read ↗

A superfamily of small potassium channel subunits: form and function of the MinK-related peptides (MiRPs).Semantic proximity Read ↗

Periodic paralysis mutation MiRP2-R83H in controls: Interpretations and general recommendation.Semantic proximity Read ↗

A Na+ channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore.Semantic proximity Read ↗

Identification and functional characterization of Kir2.6 mutations associated with non-familial hypokalemic periodic paralysis.Semantic proximity Read ↗

Mechanisms underlying the distinct K+ dependencies of periodic paralysis.Semantic proximity Read ↗

Impairment of slow inactivation as a common mechanism for periodic paralysis in DIIS4-S5.Semantic proximity Read ↗

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