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Phosphatidate phosphatase activity is induced during lipogenesis in the oleaginous yeast Yarrowia lipolytica
Author(s) -
Hardman Derell,
Ukey Rahul,
Fakas Stylianos
Publication year - 2018
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.3353
Subject(s) - lipogenesis , yarrowia , phosphatidate , biochemistry , biology , phosphatase , diacylglycerol kinase , biosynthesis , barrer , lipid metabolism , yeast , enzyme , membrane , protein kinase c , permeability (electromagnetism)
Phosphatidate (PA) phosphatase dephosphorylates the membrane phospholipid PA to diacylglycerol (DAG) that can be used for the synthesis of the storage lipid triacylglycerol (TAG). In Yarrowia lipolytica , TAG biosynthesis is induced during the lipogenic phase, which results in the accumulation of this lipid in cells. The accumulation of TAG during lipogenesis requires the supply of DAG, but the source of this DAG is not known in Y. lipolytica . In this study, the regulation of PA phosphatase during lipogenesis and its contribution to TAG biosynthesis was examined in Y. lipolytica . Lipogenesis was triggered by growing cells in high‐glucose media, whereas control cultures were grown in low‐glucose media. PA phosphatase activity increased in a time‐dependent manner as high‐glucose cells progressed in the lipogenic phase. In contrast, the activity decreased in low‐glucose cells that did not accumulate lipids. An analysis of the subcellular localization of the PA phosphatase activity showed that the membrane‐associated activity increased during lipogenesis. The significance of this increase can be explained by the fact that only the membrane‐associated PA phosphatase activity is responsible for the production of DAG. Taken together, these results indicate that PA phosphatase is involved in TAG biosynthesis during lipogenesis in Y. lipolytica .