6533b7d3fe1ef96bd125ff97

RESEARCH PRODUCT

Arabidopsis Serine Decarboxylase 1 (SDC1) in Phospholipid and Amino Acid Metabolism

Yu-chi LiuIan Sofian YunusYuki NakamuraFarrel Gunawan

subject

0301 basic medicinechemistry.chemical_classificationPhosphatidylethanolamineArabidopsis thalianaEndoplasmic reticulumPhospholipidPlant ScienceMetabolismlcsh:Plant cultureAmino acidSerineCitric acid cycle03 medical and health scienceschemistry.chemical_compound030104 developmental biologychemistryBiochemistryBiosynthesislcsh:SB1-1110phospholipid biosynthesisserine decarboxylaseglycerolipid metabolismphospholipidOriginal Research

description

Arabidopsis thaliana serine decarboxylase 1 (SDC1) catalyzes conversion of serine to ethanolamine, the first reaction step of phosphatidylcholine and phosphatidylethanolamine biosynthesis. However, an involvement of SDC1 in amino acid metabolism remains elusive despite that serine is the substrate of SDC1. Here, we showed that SDC1 localizes in mitochondria although phosphatidylcholine and phosphatidylethanolamine are known to be produced in the endoplasmic reticulum (ER). Moreover, we found that overexpression of SDC1 decreased levels of amino acid compounds derived from mitochondrial tricarboxylic acid cycle. These results suggest that mitochondria-localized SDC1 plays an important role in both phospholipid and amino acid metabolism in A. thaliana.

10.3389/fpls.2018.00972https://www.frontiersin.org/article/10.3389/fpls.2018.00972/full