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

Functional properties of the CaV1.2 calcium channel activated by calmodulin in the absence of alpha2delta subunits.

Channels (Austin, Tex.) - 1 Jan 2000

Ravindran Arippa, Kobrinsky Evgeny, Lao Qi Zong, Soldatov Nikolai M

Abstract excerpt

Voltage-activated CaV1.2 calcium channels require association of the pore-forming alpha1C subunit with accessory CaVbeta and alpha2delta subunits. Binding of a single calmodulin (CaM) to alpha1C supports Ca2+-dependent inactivation (CDI). The human CaV1.2 channel is silent in the absence of CaVbeta and/or alpha2delta. Recently, we found that coexpression of exogenous CaM (CaMex) supports plasma membrane...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Calcium Channels
Share to Calcium Channels, L-Type

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calmodulin

Share to Chlorocebus aethiops

Share to COS Cells

Share to Ion Channel Gating

Share to Membrane Potentials

Source

Open in PubMed Open full text

Identifiers

PMID: 19106618
DOI: 10.4161/chan.3.1.7498
PMCID: PMC2772127

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

Functional properties of the CaV1.2 calcium channel activated by calmodulin in the absence of alpha2delta subunits.PMID 19106618Read ↗

Differential role of the alpha1C subunit tails in regulation of the Cav1.2 channel by membrane potential, beta subunits, and Ca2+ ions.Semantic proximity Read ↗

Current modulation and membrane targeting of the calcium channel alpha1C subunit are independent functions of the beta subunit.Semantic proximity Read ↗

Identification of the components controlling inactivation of voltage-gated Ca2+ channels.Semantic proximity Read ↗

Modulation of CaV2.1 channels by Ca2+/calmodulin-dependent protein kinase II bound to the C-terminal domain.Semantic proximity Read ↗

Half-calcified calmodulin promotes basal activity and inactivation of the L-type calcium channel CaV1.2.Semantic proximity Read ↗

Ca2+/calmodulin regulates trafficking of Ca(V)1.2 Ca2+ channels in cultured hippocampal neurons.Semantic proximity Read ↗

Calcium channel alpha2delta subunits: differential expression, function, and drug binding.Semantic proximity Read ↗

Calmodulinopathy variants impair CaV1.3 and CaV2.1 regulation.Semantic proximity Read ↗

Calmodulin is the Ca2+ sensor for Ca2+ -dependent inactivation of L-type calcium channels.Semantic proximity Read ↗

Voltage Gated Calcium Channel Dysregulation May Contribute to Neurological Symptoms in CalmodulinopathiesSemantic proximity Read ↗

Regulation of maximal open probability is a separable function of Ca(v)beta subunit in L-type Ca2+ channel, dependent on NH2 terminus of alpha1C (Ca(v)1.2alpha).Semantic proximity Read ↗

Voltage-dependent calcium channels: from structure to function.Semantic proximity Read ↗

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