Newman-Smith Erin, Kourakis Matthew J, Reeves Wendy, Veeman Michael, Smith William C
Department of Molecular, Cell and Developmental Biology, University of California, Santa Barbara, Santa Barbara, United States.
Elife. 2015 Apr 13;4:e05361. doi: 10.7554/eLife.05361.
The Ciona notochord displays planar cell polarity (PCP), with anterior localization of Prickle (Pk) and Strabismus (Stbm). We report that a myosin is polarized anteriorly in these cells and strongly colocalizes with Stbm. Disruption of the actin/myosin machinery with cytochalasin or blebbistatin disrupts polarization of Pk and Stbm, but not of myosin complexes, suggesting a PCP-independent aspect of myosin localization. Wash out of cytochalasin restored Pk polarization, but not if done in the presence of blebbistatin, suggesting an active role for myosin in core PCP protein localization. On the other hand, in the pk mutant line, aimless, myosin polarization is disrupted in approximately one third of the cells, indicating a reciprocal action of core PCP signaling on myosin localization. Our results indicate a complex relationship between the actomyosin cytoskeleton and core PCP components in which myosin is not simply a downstream target of PCP signaling, but also required for PCP protein localization.
海鞘脊索显示出平面细胞极性(PCP),其中刺蛋白(Pk)和斜视蛋白(Stbm)定位于前部。我们报告称,一种肌球蛋白在这些细胞中向前部极化,并与Stbm强烈共定位。用细胞松弛素或肌球蛋白轻链激酶抑制剂破坏肌动蛋白/肌球蛋白机制会破坏Pk和Stbm的极化,但不会破坏肌球蛋白复合物的极化,这表明肌球蛋白定位存在一个不依赖于PCP的方面。洗去细胞松弛素可恢复Pk极化,但在存在肌球蛋白轻链激酶抑制剂的情况下则不能恢复,这表明肌球蛋白在核心PCP蛋白定位中发挥积极作用。另一方面,在pk突变系“无目标”中,约三分之一的细胞中肌球蛋白极化被破坏,这表明核心PCP信号对肌球蛋白定位有反向作用。我们的结果表明,肌动球蛋白细胞骨架与核心PCP成分之间存在复杂的关系,其中肌球蛋白不仅是PCP信号的下游靶点,也是PCP蛋白定位所必需的。