Bauer Reinhard, Löer Birgit, Ostrowski Katinka, Martini Julia, Weimbs Andy, Lechner Hildegard, Hoch Michael
Institute of Molecular Physiology and Developmental Biology, University of Bonn, Germany.
Chem Biol. 2005 May;12(5):515-26. doi: 10.1016/j.chembiol.2005.02.013.
Gap junctions belong to the most conserved cellular structures in multicellular organisms, from Hydra to man. They contain tightly packed clusters of hydrophilic membrane channels connecting the cytoplasms of adjacent cells, thus allowing direct communication of cells and tissues through the diffusion of ions, metabolites, and cyclic nucleotides. Recent evidence suggests that gap junctions are constructed by three different families of four transmembrane proteins: the Connexins and the Innexins found in vertebrates and in invertebrates, respectively, and the Innexin-like Pannexins, which were recently discovered in humans. This article focuses on the Drosophila Innexin multiprotein family, which is comprised of eight members. We highlight common structural features and discuss recent findings that suggest close similarities in cellular distribution, function, and regulation of Drosophila Innexins and vertebrate gap junction proteins.
间隙连接是多细胞生物中最保守的细胞结构之一，从水螅到人类皆是如此。它们包含紧密排列的亲水性膜通道簇，连接相邻细胞的细胞质，从而使细胞和组织能够通过离子、代谢物和环核苷酸的扩散进行直接通讯。最近的证据表明，间隙连接由三种不同家族的四跨膜蛋白构成：分别在脊椎动物和无脊椎动物中发现的连接蛋白（Connexins）和内向连接蛋白（Innexins），以及最近在人类中发现的类内向连接蛋白泛连接蛋白（Pannexins）。本文重点关注果蝇内向连接蛋白多蛋白家族，该家族由八个成员组成。我们强调了其共同的结构特征，并讨论了最近的研究发现，这些发现表明果蝇内向连接蛋白与脊椎动物间隙连接蛋白在细胞分布、功能和调控方面存在密切相似性。
