CaV3.1 | voltage-dependent, T type, alpha 1G 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
CaV3.1 Background Information
Overview:
CaV3.1 give rise to the T-type currents: Low-voltage-activated calcium channels are referred to as 'T' type because their currents are both transient, owing to fast inactivation, and tiny, owing to small conductance. T-type channels are thought to be involved in pacemaker activity, low-threshold calcium spikes, neuronal oscillations and resonance, and rebound burst firing. CaV3.1 channels are found in neurons and cardiac tissue. It serves pacemaking functions in both central neurons and cardiac nodal cells and supports calcium signaling in secretory cells and vascular smooth muscle. Its involvement in the modulation of firing patterns of neurons is important for information processing as well as in cell growth processes. The potentiation of CaV3.1 T-type Ca2+ channels in the inferior olive contributes to the onset of the tremor in a pharmacological model of essential tremor.
Data Sheet:
Genes:
CACNA1G
Human Protein:
UniProt O43497
Tissue:
brain neurons, cardiac nodal cells, smooth muscle cells
Function/ Application:
Ca2+pacemaker function, support calcium signalling in secretory cells and smooth muscle cells
Pathology:
Spinocerebellar ataxia 42, colorectal cancer, central pain syndrome, childhood absence epilepsy, osteogenesis imperfecta type i
Interaction:
β1-4 subunits, α2δ subunits, insulin, CaCNG3, Ras protein-specific guanine nucleotide-releasing factor 2, CaV1.2, Calsequestrin 2, TRPC5
Modulator:
Mibefradil, verapamil, zonisame, flunarizide, Bay K 8644, Nitrendipine
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
2018 - Mechanism-specific assay design facilitates the discovery of Nav1.7-selective inhibitors
SyncroPatch 768PE (a predecessor model of the SyncroPatch 384/768i) publication in PNAS
Authors:
Chernov-Rogan T., Li T., Lu G., Verschoof H., Khakh K., Jones S.W., Beresini M.H., Liu C., Ortwine D.F., McKerrall S.J., Hackos D.H., Sutherlin D., Cohen C.J., and Chen J.
2011 - Pharmacological studies of Cav3.1 T-type calcium channels using automated patch-clamp techniques
Patchliner publication in General Physiology and Biophysics (2011)
Authors:
Choi K.-H., Song C., Cheong C.S., Rhim H.
2009 - T-type channel blocking properties and antiabsence activity of two imidazo[1,2-b]pyridazine derivatives structurally related to indomethacin
Port-a-Patch publication in Neuropharmacology (2009)
Authors:
Rimoli M.G., Russo E., Cataldi M., Citraro R., Ambrosino P., Melisi D., Curcio A., De Lucia S., Patrignani P., De Sarro G., Abignente E.