Yin H L, Janmey P A, Schleicher M
Department of Physiology, University of Texas Southwestern Medical Center, Dallas.
FEBS Lett. 1990 May 7;264(1):78-80. doi: 10.1016/0014-5793(90)80769-f.
A number of Ca2(+)-activated actin filament severing proteins have been identified in eukaryotic cells of diverse lineages. Gelsolin and villin, with molecular mass of about 80-90 kDa, and severin and fragmin, with molecular mass of about 40 kDa, have been isolated from vertebrates and invertebrates, respectively. We report here a direct comparison of the functional properties of gelsolin and severin, and the finding that the actin filament severing activity of severin, like that of gelsolin, is inhibited by polyphosphoinositides. However, severin does not nucleate actin filament assembly as well as gelsolin. These characteristics are very similar to those ascribed to the NH2-terminal half of gelsolin, supporting the idea that they are evolutionarily related. Regulation of severin by polyphospholipids raises the possibility that it may participate in agonist-stimulated regulation of the actin cytoskeleton in Dictyostelium discoideum.
在不同谱系的真核细胞中已鉴定出多种Ca2+激活的肌动蛋白丝切断蛋白。凝溶胶蛋白和绒毛蛋白分子量约为80 - 90 kDa，肌动蛋白切断蛋白和肌动蛋白片段化蛋白分子量约为40 kDa，它们分别从脊椎动物和无脊椎动物中分离得到。我们在此报告凝溶胶蛋白和肌动蛋白切断蛋白功能特性的直接比较，以及发现肌动蛋白切断蛋白的肌动蛋白丝切断活性与凝溶胶蛋白一样受到多磷酸肌醇的抑制。然而，肌动蛋白切断蛋白在促进肌动蛋白丝组装方面不如凝溶胶蛋白。这些特性与归因于凝溶胶蛋白NH2末端一半的特性非常相似，支持了它们在进化上相关的观点。多磷脂对肌动蛋白切断蛋白的调节增加了它可能参与盘基网柄菌中激动剂刺激的肌动蛋白细胞骨架调节的可能性。
