Butz S, Okamoto M, Südhof T C
Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center at Dallas, 75235, USA.
Cell. 1998 Sep 18;94(6):773-82. doi: 10.1016/s0092-8674(00)81736-5.
We identify a complex of three proteins in brain that has the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion. The three proteins are: (1) CASK, a protein related to MAGUKs (membrane-associated guanylate kinases); (2) Mint1, a putative vesicular trafficking protein; and (3) Veli1, -2, and -3, vertebrate homologs of C. elegans LIN-7. CASK, Mint1, and Velis form a tight, salt-resistant complex that can be readily isolated. CASK, Mint1, and Velis contain PDZ domains in addition to other modules. However, no PDZ domains are involved in complex formation, leaving them free to recruit cell adhesion molecules, receptors, and channels to the complex. We propose that the tripartite complex acts as a nucleation site for the assembly of proteins involved in synaptic vesicle exocytosis and synaptic junctions.
我们在大脑中鉴定出一种由三种蛋白质组成的复合体，它有可能将突触小泡胞吐作用与神经元细胞黏附联系起来。这三种蛋白质分别是：（1）CASK，一种与膜相关鸟苷酸激酶（MAGUKs）相关的蛋白质；（2）Mint1，一种假定的囊泡运输蛋白；（3）Veli1、-2和-3，秀丽隐杆线虫LIN-7的脊椎动物同源物。CASK、Mint1和Velis形成一种紧密的、耐盐的复合体，很容易分离出来。CASK、Mint1和Velis除了其他模块外还含有PDZ结构域。然而，复合体的形成不涉及PDZ结构域，使得它们能够自由地招募细胞黏附分子、受体和通道到复合体中。我们提出，这个三方复合体作为一个成核位点，参与突触小泡胞吐作用和突触连接的蛋白质在此组装。
