Zerhusen B, Zhao J, Xie J, Davis P B, Ma J
Departments of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
J Biol Chem. 1999 Mar 19;274(12):7627-30. doi: 10.1074/jbc.274.12.7627.
The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together to form a single conductance pore for chloride ions.
囊性纤维化跨膜传导调节因子（CFTR）是一种受环磷酸腺苷（cAMP）依赖性蛋白激酶（PKA）和三磷酸腺苷（ATP）调节的氯离子通道，其门控过程涉及CFTR蛋白胞质结构域之间的分子内或分子间相互作用。两个CFTR分子的串联连接产生一个功能性氯离子通道，其特性与天然CFTR通道相似，包括转运至质膜、ATP和PKA依赖性门控以及8皮西门子（pS）的单位电导。由野生型和突变型CFTR组成的异二聚体也形成一个8-pS的氯离子通道，具有野生型和突变型CFTR通道的混合门控特性。数据表明，两个CFTR分子相互作用形成一个单一的氯离子传导孔。
