作者
LiWei Tu, Vincent Santarelli, ZuFang Sheng, William Skach, Debkumar Pain, Carol Deutsch
发表日期
1996/8/2
期刊
Journal of Biological Chemistry
卷号
271
期号
31
页码范围
18904-18911
出版商
American Society for Biochemistry and Molecular Biology
简介
A domain in the cytoplasmic NH2 terminus of voltage-gated K+ channels supervises the proper assembly of specific tetrameric channels (Li, M., Jan, J. M., and Jan, L. Y. (1992) Science 257, 1225-1230; Shen, N. V., Chen X., Boyer, M. M., and Pfaffinger, P. (1993) Neuron 11, 67-76). It is referred to as a first tetramerization domain, or T1 (Shen, N. V., Chen X., Boyer, M. M., and Pfaffinger, P. (1993) Neuron 11, 67-76). However, a deletion mutant of Kv1.3 that lacks the first 141 amino acids, Kv1.3 (T1−) forms functional channels, suggesting that additional association sites in the central core of Kv1.3 mediate oligomerization. To characterize these sites, we have tested the abilities of cRNA Kv1.3 (T1−) fragments co-injected with Kv1.3 (T1−) to suppress current in Xenopus oocytes. The fragments include portions of the six putative transmembrane segments, S1 through S6, specifically: S1, S1-S2, S1-S2-S3, S2-S3, S2-S3 …
引用总数
学术搜索中的文章
LW Tu, V Santarelli, ZF Sheng, W Skach, D Pain… - Journal of Biological Chemistry, 1996