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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Calcium channel, voltage-dependent, L type, alpha 1C subunit

Cav1.2, CACNA1C
This gene encodes an alpha-1 subunit of a voltage-dependent calcium channel. Calcium channels mediate the influx of calcium ions into the cell upon membrane polarization. The alpha-1 subunit consists of 24 transmembrane segments and forms the pore through which ions pass into the cell. The calcium channel consists of a complex of alpha-1, alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of these proteins, either encoded by different genes or the result of alternative splicing of transcripts. The protein encoded by this gene binds to and is inhibited by dihydropyridine. Alternative splicing results in many transcript variants encoding different proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Papers using Cav1.2 antibodies
Colocalization of fluorescent markers in confocal microscope images of plant cells.
Chien Kenneth R., In PLoS Biology, 2007
... Human Cav1.2 was obtained from Origene.
Papers on Cav1.2
Mutation of the calmodulin binding motif IQ of the L-type Ca(v)1.2 Ca2+ channel to EQ induces dilated cardiomyopathy and death.
Hofmann et al., München, Germany. In J Biol Chem, 2012
Mutation of the IQ motif to IE leads to dilated cardiomyopathy and death.
Protein phosphatase 2A effectively modulates basal L-type Ca(2+) current by dephosphorylating Ca(v)1.2 at serine 1866 in mouse cardiac myocytes.
Zhang et al., Nanjing, China. In Biochem Biophys Res Commun, 2012
these data reveal the functional role of PP2A in cardiac Ca(v)1.2 regulation.
Decreased cardiac L-type Ca²⁺ channel activity induces hypertrophy and heart failure in mice.
Molkentin et al., Cincinnati, United States. In J Clin Invest, 2012
alpha1C-/- mice subjected to pressure overload stimulation, isoproterenol infusion, and swimming showed greater cardiac hypertrophy, greater reductions in ventricular performance, and greater ventricular dilation than alpha1C+/+ controls
Single-channel monitoring of reversible L-type Ca(2+) channel Ca(V)α(1)-Ca(V)β subunit interaction.
Herzig et al., Köln, Germany. In Biophys J, 2012
HEK293alpha(1C) cells expressing the Ca(V)1.2 subunit were transiently transfected with Ca(V)alpha(2)delta1 alone or with Ca(V)beta(1a), Ca(V)beta(2b)showed increased whole-cell current and shifted the voltage dependence of activation and inactivation to hyperpolarization.
Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels.
Colecraft et al., New York City, United States. In Plos One, 2011
new mechanistic perspectives, and reveal unexpected variations in determinants, underlying inhibition of Ca(V)1.2/Ca(V)2.2 channels by distinct RGK GTPases.
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