Department of Biochemistry, Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-8725, USA.
Biochemistry. 2010 Feb 2;49(4):653-5. doi: 10.1021/bi902155t.
Voltage-gated potassium channel modulatory membrane protein KCNE3 was overexpressed and purified into both micelles and bicelles. Remarkably, microinjection of KCNE3 in bicelles into Xenopus oocytes resulted in functional co-assembly with the human KCNQ1 channel expressed therein. Microinjection of LMPC micelles containing KCNE3 did not result in channel modulation, indicating that bicelles sometimes succeed at delivering a membrane protein into a cellular membrane when classical micelles fail. Backbone NMR resonance assignments were completed for KCNE3 in both bicelles and LMPC, indicating that the secondary structure distribution in KCNE3's N-terminus and transmembrane domains exhibits only modest differences from that of KCNE1, even though these KCNE family members have very different effects on KCNQ1 channel function.
电压门控钾通道调制膜蛋白 KCNE3 被过度表达并纯化为胶束和双胶束。值得注意的是，将 KCNE3 双胶束微注射到非洲爪蟾卵母细胞中，导致其与其中表达的人 KCNQ1 通道的功能共组装。微注射含有 KCNE3 的 LMPC 胶束不会导致通道调节，表明双胶束有时在经典胶束失败时成功将膜蛋白递送到细胞膜中。KCNE3 在双胶束和 LMPC 中的骨架 NMR 共振分配已完成，表明 KCNE3 的 N 端和跨膜结构域的二级结构分布与 KCNE1 仅有适度差异，尽管这些 KCNE 家族成员对 KCNQ1 通道功能有非常不同的影响。
