ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2010
Oligomerization of Cavbeta subunits is an essential correlate of Ca2+ channel activity.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Impacts of CACNB4 overexpression on dendritic spine density in both sexes and relevance to schizophrenia.Translational psychiatry · 2024Article
- Inhibitory effects on L- and N-type calcium channels by a novel CaNaunyn-Schmiedeberg's archives of pharmacology · 2022Article
- Structural and biophysical analyses of the skeletal dihydropyridine receptor β subunit βThe Journal of biological chemistry · 2017Article
- Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channels.Frontiers in physiology · 2014Review
- Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Biochimica et biophysica acta · 2013Review
- Tetrodotoxin blockade on canine cardiac L-type Ca²⁺ channels depends on pH and redox potential.Marine drugs · 2013Article
- Cav1.2, cell proliferation, and new target in atherosclerosis.ISRN biochemistry · 2013Review
- CACNA1C (Cav1.2) in the pathophysiology of psychiatric disease.Progress in neurobiology · 2012Review
- Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.Nature reviews. Neuroscience · 2012Review
- Molecular Determinants of Cav1.2 Calcium Channel Inactivation.ISRN molecular biology · 2012Review
- Single-channel monitoring of reversible L-type Ca(2+) channel Ca(V)α(1)-Ca(V)β subunit interaction.Biophysical journal · 2011Article
- Homodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.The Journal of biological chemistry · 2011Article
- Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca ( 2+) channel β1a subunit.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Voltage-gated calcium channels conduct Ca(2+) ions in response to membrane depolarization. The resulting transient increase in cytoplasmic free calcium concentration is a critical trigger for the initiation of such vital responses as muscle contraction and transcription. L-type Ca(v)1.2 calcium channels are complexes of the pore-forming α(1C) subunit associated with cytosolic Ca(v)β subunits. All major Ca(v)βs share a highly homologous membrane associated guanylate kinase-like (MAGUK) domain that binds to α(1C) at the α-interaction domain (AID), a short motif in the linker between transmembrane repeats I and II. In this study we show that Ca(v)β subunits form multimolecular homo- and heterooligomeric complexes in human vascular smooth muscle cells expressing native calcium channels and in Cos7 cells expressing recombinant Ca(v)1.2 channel subunits. Ca(v)βs oligomerize at the α(1C) subunits residing in the plasma membrane and bind to the AID. However, Ca(v)β oligomerization occurs independently on the association with α(1C). Molecular structures responsible for Ca(v)β oligomerization reside in 3 regions of the guanylate kinase subdomain of MAGUK. An augmentation of Ca(v)β homooligomerization significantly increases the calcium current density, while heterooligomerization may also change the voltage-dependence and inactivation kinetics of the channel. Thus, oligomerization of Ca(v)β subunits represents a novel and essential aspect of calcium channel regulation.
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