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Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity
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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5299491/ https://www.ncbi.nlm.nih.gov/pubmed/27595588 http://dx.doi.org/10.1111/tpj.13321 |
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author | Craddock, Christian P. Adams, Nicolette Kroon, Johan T.M. Bryant, Fiona M. Hussey, Patrick J. Kurup, Smita Eastmond, Peter J. |
author_facet | Craddock, Christian P. Adams, Nicolette Kroon, Johan T.M. Bryant, Fiona M. Hussey, Patrick J. Kurup, Smita Eastmond, Peter J. |
author_sort | Craddock, Christian P. |
collection | PubMed |
description | 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 (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. |
format | Online Article Text |
id | pubmed-5299491 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-52994912017-02-22 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. Plant J Featured Article 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 (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. John Wiley and Sons Inc. 2016-12-01 2017-01 /pmc/articles/PMC5299491/ /pubmed/27595588 http://dx.doi.org/10.1111/tpj.13321 Text en © 2016 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Featured Article Craddock, Christian P. Adams, Nicolette Kroon, Johan T.M. Bryant, Fiona M. Hussey, Patrick J. Kurup, Smita Eastmond, Peter J. Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title | Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title_full | Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title_fullStr | Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title_full_unstemmed | Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title_short | Cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in Arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
title_sort | cyclin‐dependent kinase activity enhances phosphatidylcholine biosynthesis in arabidopsis by repressing phosphatidic acid phosphohydrolase activity |
topic | Featured Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5299491/ https://www.ncbi.nlm.nih.gov/pubmed/27595588 http://dx.doi.org/10.1111/tpj.13321 |
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