Host: The Japanese Society of Plant Physiologists
Pages 0136
Plant cytokinesis is accomplished with the formation of phragmoplast, which is formed between two daughter chromatins during anaphase. The development of phragmoplast is regulated by the MAP kinase (MAPK) cascade. Although the MAP65, one of microtubule binding proteins, has shown to be phosphorylated by MAPK, most of targets are unidentified. We have tried to identify the new targets of MAPK and found PATL2 of Arabidopsis. PATL2 contained SEC14 domain which thought to be involved in the phospholipid metabolism and vesicle transport. The recombinant PATL2 protein was phosphorylated by MAPK and showed the binding activity to phospholipids. The binding activity of the phosphorylated PALT2 was different from the native form. The GFP-fused PATL2 expressed in plant cells was localized to plasma membrane and phragmoplast. These findings suggest that PATL2 is phosphorylated by MAPK at phragmoplast during cytokinesis and that changes the composition of phospholipids on phragmoplast through the activity of PALT2.
