将各部分放在一起：CLC 阴离子通道调节的清晰明了的窗口。
Putting the pieces together: a crystal clear window into CLC anion channel regulation.
机构信息
Boylan Center for Cellular and Molecular Physiology, Mount Desert Island Biological Laboratory; Salisbury Cove, ME, USA.
出版信息
Channels (Austin). 2011 Mar-Apr;5(2):101-5. doi: 10.4161/chan.5.2.14694. Epub 2011 Mar 1.
Abstract
CLC anion transport proteins function as Cl (-) channels and Cl (-) /H (+) exchangers and are found in all major groups of life including archaebacteria. Early electrophysiological studies suggested that CLC anion channels have two pores that are opened and closed independently by a "fast" gating process operating on a millisecond timescale, and a "common" or "slow" gate that opens and closes both pores simultaneously with a timescale of seconds (Figure 1A). Subsequent biochemical and molecular experiments suggested that CLC channels/transporters are homodomeric proteins ( 1-3) .
摘要
CLC 阴离子转运蛋白作为 Cl(-) 通道和 Cl(-)/H(+) 交换器发挥作用，存在于包括古细菌在内的所有主要生命群体中。早期的电生理学研究表明，CLC 阴离子通道具有两个孔，通过毫秒级的“快速”门控过程独立打开和关闭，以及一个“共同”或“缓慢”的门，以秒为单位同时打开和关闭两个孔（图 1A）。随后的生化和分子实验表明，CLC 通道/转运蛋白是同型二聚体蛋白（1-3）。
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