Peifer M
Department of Biology, University of North Carolina, Chapel Hill 27599-3280.
J Cell Sci. 1993 Aug;105 ( Pt 4):993-1000. doi: 10.1242/jcs.105.4.993.
Sequence similarity between the Drosophila segment polarity protein Armadillo and the vertebrate adherens junction protein beta-catenin raised the possibility that adherens junctions function in transduction of intercellular signals like that mediated by Wingless/Wnt-1. To substantiate the sequence similarity, properties of Armadillo were evaluated for consistency with a junctional role. Armadillo is part of a membrane-associated complex. This complex includes Armadillo, a glycoprotein similar in size to vertebrate cadherins, and the Drosophila homolog of alpha-catenin. Armadillo co-localizes with junctions that resemble vertebrate adherens junctions in morphology and position. These results suggest that Drosophila and vertebrate adherens junctions are structurally similar, validating use of Armadillo and its associated proteins as a model for vertebrate adherens junctions.
果蝇节段极性蛋白犰狳与脊椎动物黏着连接蛋白β-连环蛋白之间的序列相似性，引发了黏着连接在细胞间信号转导中发挥作用的可能性，就像由无翅型/翼状蛋白-1介导的信号转导那样。为了证实这种序列相似性，对犰狳的特性进行了评估，以确定其与连接作用的一致性。犰狳是一种膜相关复合物的一部分。该复合物包括犰狳、一种大小与脊椎动物钙黏着蛋白相似的糖蛋白，以及α-连环蛋白的果蝇同源物。犰狳与在形态和位置上类似于脊椎动物黏着连接的连接共定位。这些结果表明，果蝇和脊椎动物的黏着连接在结构上相似，证实了将犰狳及其相关蛋白用作脊椎动物黏着连接模型的合理性。
