ArticleCellular and molecular neurobiology2007
gamma1-dependent down-regulation of recombinant voltage-gated Ca2+ channels.
Article in Cellular and molecular neurobiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Different efficiency of auxiliary/chaperone proteins to promote the functional reconstitution of honeybee glutamate and acetylcholine receptors in Xenopus laevis oocytes.Insect molecular biology · 2022Article
- Calcium current modulation by the γ1 subunit depends on alternative splicing of CaV1.1.The Journal of general physiology · 2022Article
- Regulation of high-voltage-activated CaWiley interdisciplinary reviews. Membrane transport and signaling · 2013Article
- Review
- Expression and pharmacology of endogenous Cav channels in SH-SY5Y human neuroblastoma cells.PloS one · 2013Article
- Functional coupling of Rab3-interacting molecule 1 (RIM1) and L-type Ca2+ channels in insulin release.The Journal of biological chemistry · 2011Article
- Cardiac L-type calcium channel (Cav1.2) associates with gamma subunits.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- A critical GxxxA motif in the gamma6 calcium channel subunit mediates its inhibitory effect on Cav3.1 calcium current.The Journal of physiology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
(1) Voltage-gated Ca2+ (CaV) channels are multi-subunit membrane complexes that allow depolarization-induced Ca2+ influx into cells. The skeletal muscle L-type CaV channels consist of an ion-conducting CaV1.1 subunit and auxiliary alpha2delta-1, beta1 and gamma1 subunits. This complex serves both as a CaV channel and as a voltage sensor for excitation-contraction coupling. (2) Though much is known about the mechanisms by which the alpha2delta-1 and beta1 subunits regulate CaV channel function, there is far less information on the gamma1 subunit. Previously, we characterized the interaction of gamma1 with the other components of the skeletal CaV channel complex, and showed that heterologous expression of this auxiliary subunit decreases Ca2+ current density in myotubes from gamma1 null mice. (3) In the current report, using Western blotting we show that the expression of the CaV1.1 protein is significantly lower when it is heterologously co-expressed with gamma1. Consistent with this, patch-clamp recordings showed that transient transfection of gamma1 drastically inhibited macroscopic currents through recombinant N-type (CaV2.2/alpha2delta-1/beta3) channels expressed in HEK-293 cells. (4) These findings provide evidence that co-expression of the auxiliary gamma1 subunit results in a decreased expression of the ion-conducting subunit, which may help to explain the reduction in Ca2+ current density following gamma1 transfection.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.