Peifer M, Pai L M, Casey M
Department of Biology, University of North Carolina at Chapel Hill 27599.
Dev Biol. 1994 Dec;166(2):543-56. doi: 10.1006/dbio.1994.1336.
The Drosophila segment polarity gene product Armadillo provides a link between two seemingly separate processes, regulation of segmental pattern by the Wingless intercellular signal and the function of cell-cell adherens junctions. armadillo was originally identified because of its segment polarity phenotype but subsequently was found to be the homolog of the vertebrate adherens junction protein beta-catenin. We examined the nature of the post-translational modification of Armadillo and its possible role in regulating Armadillo function. Armadillo is a phosphoprotein. Its level of phosphorylation varies both during embryonic development and from tissue to tissue. Phosphorylation occurs on both serine or threonine and tyrosine residues. Finally, Wingless signal negatively regulates Armadillo phosphorylation, while the segment polarity gene product Zeste-white 3, a serine/threonine protein kinase, promotes Armadillo phosphorylation. We discuss the implications of these results for regulation of Wingless/Wnt-1 signaling and adherens junction function.
果蝇体节极性基因产物犰狳蛋白在两个看似独立的过程之间建立了联系，即无翅细胞间信号对体节模式的调控以及细胞间黏附连接的功能。犰狳蛋白最初因其体节极性表型而被鉴定出来，但随后发现它是脊椎动物黏附连接蛋白β - 连环蛋白的同源物。我们研究了犰狳蛋白翻译后修饰的性质及其在调节犰狳蛋白功能中可能发挥的作用。犰狳蛋白是一种磷蛋白。其磷酸化水平在胚胎发育过程中以及不同组织之间都有所变化。丝氨酸或苏氨酸以及酪氨酸残基上都会发生磷酸化。最后，无翅信号对犰狳蛋白的磷酸化起负调控作用，而体节极性基因产物小体白色3（一种丝氨酸/苏氨酸蛋白激酶）则促进犰狳蛋白的磷酸化。我们讨论了这些结果对无翅/Wnt - 1信号传导调控和黏附连接功能的影响。
