2015
DOI: 10.1016/j.bbrc.2015.07.132
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Receptor protein kinase FERONIA controls leaf starch accumulation by interacting with glyceraldehyde-3-phosphate dehydrogenase

Abstract: 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 decrease… Show more

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Cited by 60 publications
(50 citation statements)
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“…The resulting high intracellular sucrose concentration, in turn, induces starch accumulation while limiting cellulose synthase activity. We also found the same phenomenon in the unrelated receptor kinase mutant feronia, for which misregulated proton/ATPase activity 5 and sucrose-sensitivity 6 has been previously reported.…”
supporting
confidence: 89%
“…The resulting high intracellular sucrose concentration, in turn, induces starch accumulation while limiting cellulose synthase activity. We also found the same phenomenon in the unrelated receptor kinase mutant feronia, for which misregulated proton/ATPase activity 5 and sucrose-sensitivity 6 has been previously reported.…”
supporting
confidence: 89%
“…8) is likely to have a much larger effect on starch accumulation in these conditions. On the other hand, we speculate that, in the absence of exogenous Suc, the hypothesis of Yang et al (2015) may be relevant, as we did observe higher levels of starch in fer in these conditions where energy is expected to be more limiting (Fig. 7D).…”
Section: Discussionmentioning
confidence: 80%
“…7, C and D). A previous report noted that fer exhibits an accumulation of starch when grown on medium containing Suc (Yang et al, 2015). The authors attributed this to an interaction between the kinase domain of FER and glyceraldehyde-3-phosphate dehydrogenase, an enzyme that would indirectly affect starch synthesis through its role in glycolysis (Yang et al, 2015).…”
Section: Discussionmentioning
confidence: 99%
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“…Additive fructose-bisphosphate aldolase, a cytoplasmic isozyme, and nonadditive glyceraldehyde-3-phosphate dehydrogenase B chloroplastic are crucial enzymes participating in the glycolytic pathway. The higher expression levels of these two proteins in hybrid offspring suggested that sorghum-sudangrass hybrids may accelerate the glycolytic pathway to enhance the function of ATP production to match its high energy demand [40,41].…”
Section: Discussionmentioning
confidence: 99%