ArticleMolecular and cellular biochemistry2003
Characterization of auto-regulation of the human cardiac alpha1 subunit of the L-type calcium channel: importance of the C-terminus.
Article in Molecular and cellular biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Protein phosphorylation maintains the normal function of cloned human CaThe Journal of general physiology · 2018Article
- Identification of a novel cAMP dependent protein kinase A phosphorylation site on the human cardiac calcium channel.Scientific reports · 2017Article
- Deletion of the distal C terminus of CaV1.2 channels leads to loss of beta-adrenergic regulation and heart failure in vivo.The Journal of biological chemistry · 2011Article
- Molecular mechanism of calcium channel regulation in the fight-or-flight response.Science signaling · 2010Article
- 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).The Journal of general physiology · 2006Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The carboxyl terminal of the L-type calcium channel alpha1C subunit comprises approximately one third of the primary structure of the alpha1 subunit (> 700 amino acids residues). This region is sensitive to limited posttranslational processing. In heart and brain the alpha1C subunits are found to be truncated but the C-terminal domain remains functionally present. Based on our previous data we hypothesized that the distal C-terminus (approximately residues 1650-1950) harbors an important, predominantly inhibitory domain. We generated C-terminal-truncated alpha1C mutants, and after expressing them in combination with a beta3 subunit in HEK-293 cells, electrophysiological experiments were carried out. In order to dissect the important inhibitory part of the C-terminus, trypsin was dialyzed into the cells. The data provide evidence that there are multiple residues within the inhibitory domain that are crucial to the inhibitory process as well as to the enhancement of expressed current by intracellular application of proteases. In addition, the expression of the chimeric mutant alpha(1C)delta1673-DRK1 demonstrated that the C-terminal is specific for the heart channel.
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Registered trials
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