Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis

作者：Yi Zhang, Nino Nikolovski, Mathias Sorieul, Tamara Vellosillo, Heather E. McFarlane, R. Dupree, Christopher Kesten, René Schneider, Carlos Driemeier, Rahul Lathe, Edwin R. Lampugnani, Xiaolan Yu, Alexander Ivakov, Monika S. Doblin, Jenny C. Mortimer, Steven P. Brown, Staffan Persson, Paul Dupree · 发表于：Nature Communications · 年份：2016 · DOI：10.1038/ncomms11656 · 被引用次数：151 · 研究领域：Polysaccharides and Plant Cell Walls、Plant nutrient uptake and metabolism、Advanced Cellulose Research Studies

As the most abundant biopolymer on Earth, cellulose is a key structural component of the plant cell wall. Cellulose is produced at the plasma membrane by cellulose synthase (CesA) complexes (CSCs), which are assembled in the endomembrane system and trafficked to the plasma membrane. While several proteins that affect CesA activity have been identified, components that regulate CSC assembly and trafficking remain unknown. Here we show that STELLO1 and 2 are Golgi-localized proteins that can interact with CesAs and control cellulose quantity. In the absence of STELLO function, the spatial distribution within the Golgi, secretion and activity of the CSCs are impaired indicating a central role of the STELLO proteins in CSC assembly. Point mutations in the predicted catalytic domains of the STELLO proteins indicate that they are glycosyltransferases facing the Golgi lumen. Hence, we have uncovered proteins that regulate CSC assembly in the plant Golgi apparatus.