A balance of capping protein and profilin functions is required to regulate actin polymerization in Drosophila bristle
A balance of capping protein and profilin functions is required to regulate actin polymerization in Drosophila bristle
复制标题
DOI：
10.1091/mbc.e02-05-0300
复制
发表时间：
2003-01-01
影响因子：
3.3
通讯作者：
Miller, KG
中科院分区：
文献类型：
--
作者：
Hopmann, R;Miller, KG
Profilin是一种已知对调节肌动蛋白丝组装很重要的特征蛋白。相对较少的研究涉及profilin如何在体内与其他肌动蛋白结合蛋白相互作用以调节复杂肌动蛋白结构的组装。为了研究profilin在分化细胞中的功能，我们研究了profilin（山雀）突变和capping蛋白（cpb）之间的遗传相互作用。封盖蛋白是细胞中封盖肌动蛋白丝倒钩末端的主要蛋白。当它在果蝇鬃毛中的功能降低时，f -肌动蛋白水平增加，肌动蛋白细胞骨架。变得无组织，导致异常刚毛形态。山雀突变抑制异常刚毛表型和相关的肌动蛋白细胞骨架异常。见于CPB突变体。此外，猪鬃中profilin的过度表达模仿了cpb功能丧失表型的许多特征。cpb与山雀之间的相互作用表明，profilin促进了肌动蛋白在刚毛中的组装，并且封顶蛋白和profilin活性之间的平衡对于f -肌动蛋白水平的适当调节是重要的。此外，这种活性平衡影响肌动蛋白结构与膜的关联，表明肌动蛋白丝动力学与细胞内肌动蛋白结构的定位之间存在联系。
Profilin is a well-characterized protein known to be important for regulating actin filament assembly. Relatively few studies have addressed how profilin interacts with other actin-binding proteins in vivo to regulate assembly of complex actin structures. To investigate the function of profilin in the context of a differentiating cell, we have studied an instructive genetic interaction between mutations in profilin (chickadee) and capping protein (cpb). Capping protein is the principal protein in cells that caps actin filament barbed ends. When its function is reduced in the Drosophila bristle, F-actin levels increase and the actin cytoskeleton. becomes disorganized, causing abnormal bristle morphology. chickadee mutations suppress the abnormal bristle phenotype and associated abnormalities of the actin cytoskeleton. seen in cpb mutants. Furthermore, overexpression of profilin in the bristle mimics many features of the cpb loss-of-function phenotype. The interaction between cpb and chickadee suggests that profilin promotes actin assembly in the bristle and that a balance between capping protein and profilin activities is important for the proper regulation of F-actin levels. Furthermore, this balance of activities affects the association of actin structures with the membrane, suggesting a link between actin filament dynamics and localization of actin structures within the cell.