大鼠lin-10与脑富集的F-肌动蛋白结合蛋白神经素-II/亲嗜素的相互作用。

Interaction of rat lin-10 with brain-enriched F-actin-binding protein, neurabin-II/spinophilin.

作者信息

Ide N, Hata Y, Hirao K, Irie M, Deguchi M, Yao I, Satoh A, Wada M, Takahashi K, Nakanishi H, Takai Y

机构信息

Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, Kobe.

出版信息

Biochem Biophys Res Commun. 1998 Mar 6;244(1):258-62. doi: 10.1006/bbrc.1998.8243.

DOI:10.1006/bbrc.1998.8243

PMID:9514910

Abstract

We have recently isolated a rat homologue of the Caenorrhabditis elegans lin-10 product. Although rat lin-10 is expressed in the cytosol and membrane fractions of various tissues, it is distributed only in the membrane fraction in brain where it is enriched in the synaptic plasma membrane and postsynaptic density fractions. We have isolated here a rat lin-10-interacting protein from rat brain and identified it to be neurabin-II/spinophilin, which has recently been isolated as a protein interacting with protein phosphatase I and F-actin. Neurabin-II/spinophilin is ubiquitously expressed but enriched in brain, especially in the synaptic plasma membrane and postsynaptic density fractions. We discuss the physiological significance of the interaction of rat lin-10 with neurabin-II/spinophilin.

摘要

我们最近分离出了秀丽隐杆线虫lin-10产物的大鼠同源物。尽管大鼠lin-10在各种组织的胞质溶胶和膜组分中都有表达，但它仅分布在大脑的膜组分中，在那里它富集于突触质膜和突触后致密组分中。我们在此从大鼠大脑中分离出一种与大鼠lin-10相互作用的蛋白，并确定其为神经肌动蛋白-II/亲肌动蛋白，该蛋白最近已作为一种与蛋白磷酸酶I和F-肌动蛋白相互作用的蛋白被分离出来。神经肌动蛋白-II/亲肌动蛋白在各处均有表达，但在大脑中富集，尤其是在突触质膜和突触后致密组分中。我们讨论了大鼠lin-10与神经肌动蛋白-II/亲肌动蛋白相互作用的生理意义。