Froehner S C
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03756.
FEBS Lett. 1989 Jun 5;249(2):229-33. doi: 10.1016/0014-5793(89)80629-5.
A cDNA clone encoding the mouse muscle postsynaptic 43 kDa protein was isolated and sequenced. The amino acid sequence of this protein, which is closely associated with nicotinic acetylcholine receptors at Torpedo electrocyte and vertebrate skeletal muscle synapses, is very similar in different species. A cysteine-rich region homologous to part of the regulatory domain of protein kinase C may be important in interactions of this protein with the lipid bilayer. RNA transcripts for the 43 kDa protein increase only 2-3 fold after denervation of rat skeletal muscle, in sharp contrast to the alpha-subunit of the muscle nicotinic receptor which increases more than 30-fold. Thus, the expression of these two proteins is regulated by different mechanisms.
分离并测序了一个编码小鼠肌肉突触后43kDa蛋白的cDNA克隆。该蛋白的氨基酸序列与电鳐电细胞和脊椎动物骨骼肌突触处的烟碱型乙酰胆碱受体密切相关,在不同物种中非常相似。与蛋白激酶C调节域部分同源的富含半胱氨酸区域可能在该蛋白与脂质双层的相互作用中起重要作用。大鼠骨骼肌去神经支配后,43kDa蛋白的RNA转录本仅增加2 - 3倍,这与肌肉烟碱型受体α亚基增加超过30倍形成鲜明对比。因此,这两种蛋白的表达受不同机制调控。