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Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity
Author(s) -
Craddock Christian P.,
Adams Nicolette,
Kroon Johan T.M.,
Bryant Fiona M.,
Hussey Patrick J.,
Kurup Smita,
Eastmond Peter J.
Publication year - 2017
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13321
Subject(s) - phosphatidic acid , endomembrane system , cyclin dependent kinase , microbiology and biotechnology , biochemistry , biology , arabidopsis , kinase , endoplasmic reticulum , chemistry , cell cycle , phospholipid , golgi apparatus , cell , mutant , membrane , gene
Summary Coordination of endomembrane biogenesis with cell cycle progression is considered to be important in maintaining cell function during growth and development. We previously showed that the disruption of PHOSPHATIDIC ACID PHOSPHOHYDROLASE ( PAH ) activity in Arabidopsis thaliana stimulates biosynthesis of the major phospholipid phosphatidylcholine ( PC ) and causes expansion of the endoplasmic reticulum. Here we show that PC biosynthesis is repressed by disruption of the core cell cycle regulator CYCLIN ‐ DEPENDENT KINASE A;1 ( CDKA ;1) and that this repression is reliant on PAH . Furthermore, we show that cyclin‐dependent kinases ( CDK s) phosphorylate PAH 1 at serine 162, which reduces both its activity and membrane association. Expression of a CDK ‐insensitive version of PAH 1 with a serine 162 to alanine substitution represses PC biosynthesis and also reduces the rate of cell division in early leaf development. Together our findings reveal a physiologically important mechanism that couples the rate of phospholipid biosynthesis and endomembrane biogenesis to cell cycle progression in Arabidopsis.