共 41 条
Transfer of β subunit regulation from high to low voltage-gated Ca2+ channels
被引:45
作者:

Arias, JM
论文数: 0 引用数: 0
h-index: 0
机构: Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA

Murbartián, J
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h-index: 0
机构: Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA

Vitko, I
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h-index: 0
机构: Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA

Lee, JH
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h-index: 0
机构: Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA

Perez-Reyes, E
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h-index: 0
机构:
Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA
机构:
[1] Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA
[2] Sogang Univ, Dept Life Sci, Seoul 121742, South Korea
来源:
FEBS LETTERS
|
2005年
/
579卷
/
18期
关键词:
calcium channels;
N-type;
T-type;
ion channel gating;
structure-activity relationship;
D O I:
10.1016/j.febslet.2005.06.008
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
High voltage-activated Ca2+ channel expression and gating is controlled by their beta subunits. Although the sites of interaction are known at the atomic level, how beta modulates gating remains to be determined. Using a chimeric approach, beta subunit regulation was conferred to a low voltage-activated channel. Regulation was dependent on a rigid linker connecting the a, interaction domain to IS6. Chimeric channels also revealed a role for IS6 in channel gating. Taken together, these results support a direct coupling model where beta subunits alter movements in IS6 that occur as the channel transits between closed, open, and inactivated states. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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收藏
页码:3907 / 3912
页数:6
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