Actomyosin and CSI1/POM2 cooperate to deliver cellulose synthase from Golgi to cortical microtubules in Arabidopsis.

As one of the major components of plant cell walls, cellulose is crucial for plant growth and development. Cellulose is synthesized by cellulose synthase (CesA) complexes (CSCs), which are trafficked and delivered from the Golgi apparatus to the plasma membrane. How CesAs are released from Golgi remains largely unclear. In this study, we observed that STELLO (STL) family proteins localized at a group of small CesA-containing compartments called Small CesA compartments (SmaCCs) or microtubule-associated CesA compartments (MASCs). The STL-labeled SmaCCs/MASCs were directly derived from Golgi through a membrane-stretching process: membrane-patches of Golgi attached to cortical microtubules, which led to emergence of membrane-tails that finally ruptured to generate SmaCCs/MASCs associated with the cortical microtubules. While myosin propelled the movement of Golgi along actin filaments to stretch the tails, the CesA-microtubule linker protein, CSI1/POM2 was indispensable for the tight anchor of the membrane-tail ends at cortical microtubules. Together, our data reveal a non-canonical delivery route to the plasma membrane of a major enzyme complex in plant biology.