Department of Biology and Center for Engineering Mechanobiology, Washington University in St. Louis, Missouri 63130.
Department of Biology and Center for Engineering Mechanobiology, Washington University in St. Louis, Missouri 63130
Plant Cell. 2020 Aug;32(8):2508-2524. doi: 10.1105/tpc.19.00700. Epub 2020 Jun 2.
Cell wall assembly requires harmonized deposition of cellulose and matrix polysaccharides. Cortical microtubules orient the deposition of cellulose by guiding the trajectory of cellulose synthase complexes. Vesicles containing matrix polysaccharides are thought to be transported by the FRAGILE FIBER1 (FRA1) kinesin to facilitate their secretion along cortical microtubules. The cortical microtubule cytoskeleton thus may provide a platform to coordinate the delivery of cellulose and matrix polysaccharides, but the underlying molecular mechanisms remain unknown. Here, we show that the tail region of the Arabidopsis () FRA1 kinesin physically interacts with cellulose synthase-microtubule uncoupling (CMU) proteins that are important for the microtubule-dependent guidance of cellulose synthase complexes. Interaction with CMUs did not affect microtubule binding or motility of the FRA1 kinesin but differentially affected the protein levels and microtubule localization of CMU1 and CMU2, thus regulating the lateral stability of cortical microtubules. Phosphorylation of the FRA1 tail region inhibited binding to CMUs and consequently reversed the extent of cortical microtubule decoration by CMU1 and CMU2. Genetic experiments demonstrated the significance of this interaction to the growth and reproduction of Arabidopsis plants. We propose that modulation of CMU protein levels and microtubule localization by FRA1 provides a mechanism that stabilizes the sites of deposition of both cellulose and matrix polysaccharides.
细胞壁的组装需要纤维素和基质多糖的沉积协调进行。皮层微管通过指导纤维素合酶复合物的轨迹来定向纤维素的沉积。含有基质多糖的囊泡被认为是通过脆弱纤维 1(FRA1)驱动蛋白运输的,以促进它们沿着皮层微管的分泌。因此,皮层微管细胞骨架可能为协调纤维素和基质多糖的输送提供了一个平台,但潜在的分子机制仍不清楚。在这里,我们表明,拟南芥()FRA1 驱动蛋白的尾部区域与纤维素合酶-微管解偶联(CMU)蛋白发生物理相互作用,CMU 蛋白对于纤维素合酶复合物的微管依赖性导向很重要。与 CMUs 的相互作用不影响微管结合或 FRA1 驱动蛋白的运动性,但对 CMU1 和 CMU2 的蛋白水平和微管定位有不同的影响,从而调节皮层微管的侧向稳定性。FRA1 尾部区域的磷酸化抑制了与 CMUs 的结合,从而逆转了 CMU1 和 CMU2 对皮层微管的装饰程度。遗传实验证明了这种相互作用对拟南芥植物生长和繁殖的重要性。我们提出,FRA1 对 CMU 蛋白水平和微管定位的调节提供了一种稳定纤维素和基质多糖沉积位点的机制。