Photosynthetic activity influences cellulose biosynthesis and phosphorylation of proteins involved therein in Arabidopsis leaves

© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 65(2014), 17 vom: 29. Sept., Seite 4997-5010
1. Verfasser: Boex-Fontvieille, Edouard (VerfasserIn)
Weitere Verfasser: Davanture, Marlène, Jossier, Mathieu, Zivy, Michel, Hodges, Michael, Tcherkez, Guillaume
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis cellulose phosphoproteomics photosynthesis protein phosphorylation. Arabidopsis Proteins Cellulose 9004-34-6
Beschreibung
Zusammenfassung:© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
Cellulose is one of the most important organic compounds in terrestrial ecosystems and represents a major plant structural polymer. However, knowledge of the regulation of cellulose biosynthesis is still rather limited. Recent studies have shown that the phosphorylation of cellulose synthases (CESAs) may represent a key regulatory event in cellulose production. However, the impact of environmental conditions on the carbon flux of cellulose deposition and on phosphorylation levels of CESAs has not been fully elucidated. Here, we took advantage of gas exchange measurements, isotopic techniques, metabolomics, and quantitative phosphoproteomics to investigate the regulation of cellulose production in Arabidopsis rosette leaves in different photosynthetic contexts (different CO2 mole fractions) or upon light/dark transition. We show that the carbon flux to cellulose production increased with photosynthesis, but not proportionally. The phosphorylation level of several phosphopeptides associated with CESA1 and 3, and several enzymes of sugar metabolism was higher in the light and/or increased with photosynthesis. By contrast, a phosphopeptide (Ser126) associated with CESA5 seemed to be more phosphorylated in the dark. Our data suggest that photosynthetic activity affects cellulose deposition through the control of both sucrose metabolism and cellulose synthesis complexes themselves by protein phosphorylation
Beschreibung:Date Completed 28.05.2015
Date Revised 16.10.2014
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/eru268