Betto Giulia, Cherian O Lijo, Pifferi Simone, Cenedese Valentina, Boccaccio Anna, Menini Anna
Neurobiology Group, International School for Advanced Studies (SISSA), 34136 Trieste, Italy.
Istituto di Biofisica, Consiglio Nazionale delle Ricerche, 16149 Genova, Italy
J Gen Physiol. 2014 Jun;143(6):703-18. doi: 10.1085/jgp.201411182.
At least two members of the TMEM16/anoctamin family, TMEM16A (also known as anoctamin1) and TMEM16B (also known as anoctamin2), encode Ca(2+)-activated Cl(-) channels (CaCCs), which are found in various cell types and mediate numerous physiological functions. Here, we used whole-cell and excised inside-out patch-clamp to investigate the relationship between anion permeation and gating, two processes typically viewed as independent, in TMEM16B expressed in HEK 293T cells. The permeability ratio sequence determined by substituting Cl(-) with other anions (PX/PCl) was SCN(-) > I(-) > NO3 (-) > Br(-) > Cl(-) > F(-) > gluconate. When external Cl(-) was substituted with other anions, TMEM16B activation and deactivation kinetics at 0.5 µM Ca(2+) were modified according to the sequence of permeability ratios, with anions more permeant than Cl(-) slowing both activation and deactivation and anions less permeant than Cl(-) accelerating them. Moreover, replacement of external Cl(-) with gluconate, or sucrose, shifted the voltage dependence of steady-state activation (G-V relation) to more positive potentials, whereas substitution of extracellular or intracellular Cl(-) with SCN(-) shifted G-V to more negative potentials. Dose-response relationships for Ca(2+) in the presence of different extracellular anions indicated that the apparent affinity for Ca(2+) at +100 mV increased with increasing permeability ratio. The apparent affinity for Ca(2+) in the presence of intracellular SCN(-) also increased compared with that in Cl(-). Our results provide the first evidence that TMEM16B gating is modulated by permeant anions and provide the basis for future studies aimed at identifying the molecular determinants of TMEM16B ion selectivity and gating.
跨膜蛋白16/anoctamin家族的至少两个成员,即跨膜蛋白16A(也称为anoctamin1)和跨膜蛋白16B(也称为anoctamin2),编码钙激活氯离子通道(CaCCs),这些通道存在于多种细胞类型中,并介导众多生理功能。在此,我们运用全细胞和内面向外膜片钳技术,研究了在HEK 293T细胞中表达的跨膜蛋白16B中,阴离子通透与门控这两个通常被视为相互独立的过程之间的关系。用其他阴离子替代氯离子(PX/PCl)所确定的通透率序列为:硫氰酸根离子(SCN⁻)>碘离子(I⁻)>硝酸根离子(NO₃⁻)>溴离子(Br⁻)>氯离子(Cl⁻)>氟离子(F⁻)>葡萄糖酸盐。当外部氯离子被其他阴离子替代时,在0.5 μM钙离子条件下,跨膜蛋白16B的激活和失活动力学根据通透率序列发生改变,比氯离子更具通透性的阴离子会减慢激活和失活速度,而比氯离子通透性更低的阴离子则会加速它们。此外,用葡萄糖酸盐或蔗糖替代外部氯离子会使稳态激活的电压依赖性(G-V关系)向更正的电位偏移,而用硫氰酸根离子替代细胞外或细胞内的氯离子会使G-V向更负的电位偏移。在不同细胞外阴离子存在的情况下,钙离子的剂量-反应关系表明,在+100 mV时对钙离子的表观亲和力随通透率增加而升高。与在氯离子存在时相比,细胞内存在硫氰酸根离子时对钙离子的表观亲和力也增加了。我们的结果首次证明跨膜蛋白16B的门控受通透阴离子的调节,并为未来旨在确定跨膜蛋白16B离子选择性和门控的分子决定因素的研究提供了基础。