TY - JOUR
T1 - The roles of the subunits in the function of the calcium channel
AU - Singer, Dafna
AU - Biel, Martin
AU - Lotan, Ilana
AU - Flockerzi, Veit
AU - Hofmann, Franz
AU - Dascal, Nathan
PY - 1991
Y1 - 1991
N2 - Dihydropyridine-sensitive voltage-dependent L-type calcium channels are critical to excitation-secretion and excitation-contraction coupling. The channel molecule is a complex of the main, pore-forming subunit α1 and four additional subunits: α2, δ, β, and γ (α2 and δ are encoded by a single messenger RNA). The α1 subunit messenger RNA alone directs expression of functional calcium channels in Xenopus oocytes, and coexpression of the α2/δ and β subunits enhances the amplitude of the current. The α2, δ, and γ subunits also have pronounced effects on its macroscopic characteristics, such as kinetics, voltage dependence of activation and inactivation, and enhancement by a dihydropyridine agonist. In some cases, specific modulatory functions can be assigned to individual subunits, whereas in other cases the different subunits appear to act in concert to modulate the properties of the channel.
AB - Dihydropyridine-sensitive voltage-dependent L-type calcium channels are critical to excitation-secretion and excitation-contraction coupling. The channel molecule is a complex of the main, pore-forming subunit α1 and four additional subunits: α2, δ, β, and γ (α2 and δ are encoded by a single messenger RNA). The α1 subunit messenger RNA alone directs expression of functional calcium channels in Xenopus oocytes, and coexpression of the α2/δ and β subunits enhances the amplitude of the current. The α2, δ, and γ subunits also have pronounced effects on its macroscopic characteristics, such as kinetics, voltage dependence of activation and inactivation, and enhancement by a dihydropyridine agonist. In some cases, specific modulatory functions can be assigned to individual subunits, whereas in other cases the different subunits appear to act in concert to modulate the properties of the channel.
UR - http://www.scopus.com/inward/record.url?scp=0025942910&partnerID=8YFLogxK
U2 - 10.1126/science.1716787
DO - 10.1126/science.1716787
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C2 - 1716787
AN - SCOPUS:0025942910
SN - 0036-8075
VL - 253
SP - 1553
EP - 1557
JO - Science
JF - Science
IS - 5027
ER -