CaV2.1 | voltage-dependent, P/Q-type, alpha 1A subunit calcium channel
Family:
Calcium channels
Subgroups:
L-Type (CaV1.1–CaV1.4), P/Q-Type (CaV2.1), N-Type (CaV2.2), R-Type (CaV2.3), T-Type (CaV3.1–CaV3.3)
Topology:
Six transmembrane alpha helices (S1–S6), total of four homologous domains make up the tetrameric alpha subunit structure
Assembling:
One large alpha subunit forms a functional channel, accessory subunits ( α1, α2δ, β1-4, and γ) are crucial for robust expression, they functionally modulate the alpha subunit
CaV2.1 Background Information
Overview:
CaV2.1, also known as brain calcium channel I, gives rise to P and/or Q-type calcium currents and is predominantly expressed in neuronal tissue. Localized to the presynaptic membrane of many types of neurons, CaV2.1 ion channels are involved in triggering neurotransmitter release via both, vesicle release and postsynaptic calcium entry.
Data Sheet:
Gene:
CACNA1A
Human Protein:
UniProt O00555
Tissue:
Brain
Function/ Application:
Pre-synaptic Ca2+ influx and neurotransmitter release in neurons, fast synaptic transmission
Pathology:
Migraine (FHM-1), ataxia (EA-2, SCA6), Benign paroxysmal torticollis of infancy, hemiplegia
Interaction:
β4 subunit CACNB4, α2δ subunits, calmodulin, CaBP1, VILIP, mint, CASK, Syntaxin, SNAP25
Modulator:
Kuratoxin, ω-agatoxin IIIA, ω-conotoxin MVIIC, ω-agatoxin-IVA, roscovitine
Assays:
Patch Clamp: whole cell, room temperature
Particularities:
CaV channels often show a rundown phenomenon. Adequate intra- and extracellular solutions are essential for a good data quality.
Reviews and Links
Recommended Reviews:
Transporter classification database:
UniProt:
IUPHAR/PBS:
Publications
2015 - Golgi anti-apoptotic proteins are highly conserved Ion Channels That Affect Apoptosis and Cell Migration
Port-a-Patch and 
Vesicle Prep Pro publication in Journal of Biological Chemistry (2015)
Authors:
Carrara G., Saraiva N., Parsons M., Byrne B., Prole D.L., Taylor C.W., Smith G.L.
2013 - Establishment of a Secondary Screening Assay for P/Q-Type Calcium Channel Blockers
Patchliner publication in Combinatorial Chemistry & High Throughput Screening (2013)
Authors:
Hermann D., Mezler M., Swensen A., Bruehl C., Obergrußberger A., Wicke K., Schoemaker H., Gross G., Draguhn A., Nimmrich V.
Webinars
28.04.2020 | Webinar: Validation and optimization of automated patch clamp voltage-gated Ca2+ channel assays
Patchliner Webinar
Date: April 28. 2020, 4:00 PM CET (10:00 AM EDT)
Marc will outline the development, optimization and validation of a range of voltage-gated Ca2+ channel assays on the Patchliner automated patch clamp platform that were subsequently used in an 8 year drug discovery collaboration between Metrion Biosciences and a german pharma company.
Speakers:
Dr. Marc Rogers (Chief Scientific Officer, Metrion Biosciences)
Dr. András Horváth (Application Scientist, Nanion Technologies)
20.11.2018 | Webinar: The RELEVANCE of ion channel interplay – Voltage-activated channels in non-excitable cells
SyncroPatch 384PE (a predecessor model of SyncroPatch 384i), Patchliner, 
Port-a-Patch Webinar
Date: November 20. 2018, 4:00 PM CET (11:00 AM EDT)
The Webinar focuses on the automated patch clamp assay development for the study of red blood cells in health and disease and the RELEVANCE project, an international consortium of 13 partners from academia, diagnostic labs, blood supply centers, and small companies that combines basic and translational research to improve prognostic, diagnostic and therapeutic approaches on red blood cell function in health and disease. To this end, Nanion contributes assays for the electrophysiological characterization of healthy and patient-derived red blood cells.
07.09.2021 | Webinar: Automated patch clamp assay development for the study of red blood cells (RBCs) in health and disease
SyncroPatch 384, Patchliner, Port-a-Patch Webinar
Date: September 07. 2021, 4:00 PM CEST (10:00 AM EDT)
Abstract:
Calcium (Ca2+) is a universal signalling molecule and is critically important in regulating many physiological functions and survival of RBCs. Amongst others, intracellular Ca2+ controls cell volume and deformability. This process plays a substantial role in RBCs since their volume needs to adapt when passing blood vessel constrictions during the flow. Excessive Ca2+ uptake also leads to accelerated cell clearance causing anaemia.
Therefore, studying Ca2+ regulation is crucial to understand RBC diseases. Piezo1, KCa3.1 (Gardos channel) and NMDA receptors are three channels present in the RBC membrane and critical for Ca2+ regulation.
We developed functional assays to measure these channels in healthy and diseased RBCs populations using electrophysiological tools, contributing to the characterization of RBC diseases.