Cyclin-dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity

Craddock, Christian P.; Adams, Nicolette; Kroon, Johan T.M.; Bryant, Fiona M.; Hussey, Patrick J.; Kurup, Smita; Eastmond, Peter J.

Abstract

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 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 CDKs phosphorylate PAH1 at serine 162, which reduces both its activity and membrane association. Expression of a CDK-insensitive version of PAH1 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.

Citation

Craddock, C. P., Adams, N., Kroon, J. T., Bryant, F. M., Hussey, P. J., Kurup, S., & Eastmond, P. J. (2017). Cyclin-dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity. The Plant Journal, 89(1), 3-14. https://doi.org/10.1111/tpj.13321

• Journal Article Type: Article
• Acceptance Date: Aug 24, 2016
• Online Publication Date: Dec 1, 2016
• Publication Date: 2017-01
• Deposit Date: Sep 19, 2016
• Publicly Available Date: Sep 19, 2016
• Journal: Plant Journal
• Print ISSN: 0960-7412
• Electronic ISSN: 1365-313X
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 89
• Issue: 1
• Pages: 3-14
• DOI: https://doi.org/10.1111/tpj.13321
• Public URL: https://durham-repository.worktribe.com/output/1376371