Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor

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	Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor
	Li H(李辉) ; Yao J(姚镜) ; Tong XT(童孝田) ; Guo ZH(郭兆华) ; Wu Y(吴英) ; Sun L(孙亮) ; Pan N(潘娜) ; Wu HM(吴厚铭) ; Xu T(徐滔) ; Ding JP(丁久平)
刊名	J. Biol. Chem.
	2007
卷号	282 期号:24 页码:17720-17728
ISSN号	0021-9258
其他题名	用三残基探针探测钾离子通道Slo1孔道与第二亚单元NH2末端相互作用位点
通讯作者	丁久平
英文摘要	Calcium- and voltage-gated (BK) K+ channels encoded by Slo1 play an essential role in nervous systems. Although it shares many common features with voltage-dependent KV channels, the BK channel exhibits differences in gating and inactivation. Using a mutant in which FWI replaces three residues (FIW) in the NH2 terminus of wild-type beta 2-subunits, in conjunction with alanine-scanning mutagenesis of the Slo1 S6 segment, we identify that the NH2 terminus of beta 2-subunits interacts with the residues near the cytosolic superficial mouth of BK channels during inactivation. The cytosolic blockers did not share the sites with NH2 terminus of beta 2-subunits. A novel blocking-inactivating scheme was proposed to account for the observed noncompetition inactivation. Our results also suggest that the residue Ile-323 plays a dual role in interacting with the NH2 terminus of beta 2-subunits and modulating the gating of BK channels.
学科主题	生命有机化学
收录类别	SCI
原文出处	http://dx.doi.org/10.1074/jbc.M607063200
语种	英语
WOS记录号	WOS:000247084500045
公开日期	2013-02-21
内容类型	期刊论文
源URL	[http://202.127.28.38/handle/331003/17381]
专题	上海有机化学研究所_上海有机化学研究所
推荐引用方式 GB/T 7714	Li H,Yao J,Tong XT,et al. Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor[J]. J. Biol. Chem.,2007,282(24):17720-17728.
APA	李辉.,姚镜.,童孝田.,郭兆华.,吴英.,...&丁久平.(2007).Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor.J. Biol. Chem.,282(24),17720-17728.
MLA	李辉,et al."Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor".J. Biol. Chem. 282.24(2007):17720-17728.