Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Craddock, Christian P., Adams, Nicolette, Kroon, Johan T.M., Bryant, Fiona M., Hussey, Patrick J., Kurup, Smita, Eastmond, Peter J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
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
_version_ 1782506036342554624
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
work_keys_str_mv AT craddockchristianp cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT adamsnicolette cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT kroonjohantm cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT bryantfionam cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT husseypatrickj cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT kurupsmita cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity
AT eastmondpeterj cyclindependentkinaseactivityenhancesphosphatidylcholinebiosynthesisinarabidopsisbyrepressingphosphatidicacidphosphohydrolaseactivity