Mercado Jose, Czajkowski Cynthia
Department of Physiology, University of Wisconsin-Madison, 601 Science Drive, Madison, WI 53706, USA.
J Biol Chem. 2008 May 30;283(22):15250-7. doi: 10.1074/jbc.M708638200. Epub 2008 Apr 3.
Gamma-aminobutyric acid (GABA) binding to GABA(A) receptors (GABA(A)Rs) triggers conformational movements in the alpha(1) and beta(2) pre-M1 regions that are associated with channel gating. At high concentrations, the barbiturate pentobarbital opens GABA(A)R channels with similar conductances as GABA, suggesting that their open state structures are alike. Little, however, is known about the structural rearrangements induced by barbiturates. Here, we examined whether pentobarbital activation triggers movements in the GABA(A)R pre-M1 regions. Alpha(1)beta(2) GABA(A)Rs containing cysteine substitutions in the pre-M1 alpha(1) (K219C, K221C) and beta(2) (K213C, K215C) subunits were expressed in Xenopus oocytes and analyzed using two-electrode voltage clamp. The cysteine substitutions had little to no effect on GABA and pentobarbital EC(50) values. Tethering chemically diverse thiol-reactive methanethiosulfonate reagents onto alpha(1)K219C and alpha(1)K221C affected GABA- and pentobarbital-activated currents differently, suggesting that the pre-M1 structural elements important for GABA and pentobarbital current activation are distinct. Moreover, pentobarbital altered the rates of cysteine modification by methanethiosulfonate reagents differently than GABA. For alpha(1)K221Cbeta(2) receptors, pentobarbital decreased the rate of cysteine modification whereas GABA had no effect. For alpha(1)beta(2)K215C receptors, pentobarbital had no effect whereas GABA increased the modification rate. The competitive GABA antagonist SR-95531 and a low, non-activating concentration of pentobarbital did not alter their modification rates, suggesting that the GABA- and pentobarbital-mediated changes in rates reflect gating movements. Overall, the data indicate that the pre-M1 region is involved in both GABA- and pentobarbital-mediated gating transitions. Pentobarbital, however, triggers different movements in this region than GABA, suggesting their activation mechanisms differ.
γ-氨基丁酸(GABA)与GABA A受体(GABA A Rs)结合会触发α(1)和β(2)预M1区域的构象运动,这些运动与通道门控相关。在高浓度下,巴比妥类药物戊巴比妥打开GABA A R通道的电导与GABA相似,这表明它们的开放状态结构相似。然而,关于巴比妥类药物引起的结构重排知之甚少。在这里,我们研究了戊巴比妥激活是否会触发GABA A R预M1区域的运动。在非洲爪蟾卵母细胞中表达在预M1α(1)(K219C、K221C)和β(2)(K213C、K215C)亚基中含有半胱氨酸替代的α(1)β(2) GABA A Rs,并使用双电极电压钳进行分析。半胱氨酸替代对GABA和戊巴比妥的半数有效浓度(EC 50)值几乎没有影响。将化学性质不同的硫醇反应性甲硫基磺酸盐试剂连接到α(1)K219C和α(1)K221C上对GABA和戊巴比妥激活的电流影响不同,这表明对GABA和戊巴比妥电流激活重要的预M1结构元件是不同的。此外,戊巴比妥改变甲硫基磺酸盐试剂对半胱氨酸修饰的速率与GABA不同。对于α(1)K221Cβ(2)受体,戊巴比妥降低了半胱氨酸修饰的速率,而GABA没有影响。对于α(1)β(2)K215C受体,戊巴比妥没有影响,而GABA增加了修饰速率。竞争性GABA拮抗剂SR-95531和低浓度、非激活浓度的戊巴比妥没有改变它们的修饰速率,这表明GABA和戊巴比妥介导的速率变化反映了门控运动。总体而言,数据表明预M1区域参与了GABA和戊巴比妥介导的门控转变。然而,戊巴比妥在该区域触发的运动与GABA不同,这表明它们的激活机制不同。