S-Acylation of the cellulose synthase complex is essential for its plasma membrane localization

作者：Manoj Kumar, Raymond Wightman, Ivan Atanassov, Anjali Gupta, Charlotte H. Hurst, Piers A. Hemsley, Simon R. Turner · 发表于：Science · 年份：2016 · DOI：10.1126/science.aaf4009 · 被引用次数：93 · 研究领域：Polysaccharides and Plant Cell Walls、Advanced Cellulose Research Studies、Plant nutrient uptake and metabolism

Plant cellulose microfibrils are synthesized by a process that propels the cellulose synthase complex (CSC) through the plane of the plasma membrane. How interactions between membranes and the CSC are regulated is currently unknown. Here, we demonstrate that all catalytic subunits of the CSC, known as cellulose synthase A (CESA) proteins, are S-acylated. Analysis of Arabidopsis CESA7 reveals four cysteines in variable region 2 (VR2) and two cysteines at the carboxy terminus (CT) as S-acylation sites. Mutating both the VR2 and CT cysteines permits CSC assembly and trafficking to the Golgi but prevents localization to the plasma membrane. Estimates suggest that a single CSC contains more than 100 S-acyl groups, which greatly increase the hydrophobic nature of the CSC and likely influence its immediate membrane environment.