Receptor protein kinase FERONIA controls leaf starch accumulation by interacting with glyceraldehyde-3-phosphate dehydrogenase

• DOI: 10.1016/j.bbrc.2015.07.132
• Publication Date: 2015-07-29T19:19:58Z
• Authors: Tao Yang; Long Wang; Chiyu Li; Ying Liu; Sirui Zhu; Yinyao Qi; Xuanming Liu; Qinglu Lin; Sheng Luan; Feng Yu
• Keywords: 0301 basic medicine; Sucrose; Arabidopsis Proteins; Phosphotransferases; Arabidopsis; Oryza; Starch; Isoenzymes; Plant Leaves; 03 medical and health sciences; Gene Expression Regulation, Plant; Seedlings; Two-Hybrid System Techniques; Mannitol; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Energy Metabolism; Protein Binding; Signal Transduction

Cell expansion is coordinated by several cues, but available energy is the major factor determining growth. Receptor protein kinase FERONIA (FER) is a master regulator of cell expansion, but the details of its control mechanisms are not clear. Here we show that FER interacts with cytosolic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH, GAPC1 and GAPC2), that catalyzes a key reaction in glycolysis, which contributes to energy production. When there is an FER deficiency, there are corresponding decreases in the enzyme activity of GAPDH and increased amounts of starch. More importantly, gapc1/2 mutants mimic fer4 mutants. These data indicate that FER regulated starch content is an evolutionarily conserved function in plants that connects the cell expansion and energy metabolism pathways.