Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms
- Author
- Lam Dai Vu (UGent) , Tingting Zhu (UGent) , Inge Verstraeten (UGent) , Brigitte Van De Cotte (UGent) , Kris Gevaert (UGent) and Ive De Smet (UGent)
- Organization
- Abstract
- Wheat (Triticum ssp.) is one of the most important human food sources. However, this crop is very sensitive to temperature changes. Specifically, processes during wheat leaf, flower, and seed development and photosynthesis, which all contribute to the yield of this crop, are affected by high temperature. While this has to some extent been investigated on physiological, developmental, and molecular levels, very little is known about early signalling events associated with an increase in temperature. Phosphorylation-mediated signalling mechanisms, which are quick and dynamic, are associated with plant growth and development, also under abiotic stress conditions. Therefore, we probed the impact of a short-term and mild increase in temperature on the wheat leaf and spikelet phosphoproteome. In total, 3822 (containing 5178 phosphosites) and 5581 phosphopeptides (containing 7023 phosphosites) were identified in leaf and spikelet samples, respectively. Following statistical analysis, the resulting data set provides the scientific community with a first large-scale plant phosphoproteome under the control of higher ambient temperature. This community resource on the high temperature-mediated wheat phosphoproteome will be valuable for future studies. Our analyses also revealed a core set of common proteins between leaf and spikelet, suggesting some level of conserved regulatory mechanisms. Furthermore, we observed temperature-regulated interconversion of phosphoforms, which probably impacts protein activity.
- Keywords
- TRITICUM-AESTIVUM L., HEAT-STRESS, PROTEIN-PHOSPHORYLATION, MOLECULAR-MECHANISMS, ABIOTIC STRESS, REPRODUCTIVE DEVELOPMENT, ARABIDOPSIS-THALIANA, RESPONSIVE PROTEINS, FREEZING TOLERANCE, PROTEOMIC, ANALYSIS, Leaf, phosphoproteomics, phosphorylation, signalling, spikelet, temperature, wheat
Downloads
-
Vu et al. (2018) Journal of Experimental Botany 69,4609.pdf
- full text
- |
- open access
- |
- |
- 3.36 MB
Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8575894
- MLA
- Vu, Lam Dai, et al. “Temperature-Induced Changes in the Wheat Phosphoproteome Reveal Temperature-Regulated Interconversion of Phosphoforms.” JOURNAL OF EXPERIMENTAL BOTANY, vol. 69, no. 19, 2018, pp. 4609–24, doi:10.1093/jxb/ery204.
- APA
- Vu, L. D., Zhu, T., Verstraeten, I., Van De Cotte, B., Gevaert, K., & De Smet, I. (2018). Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms. JOURNAL OF EXPERIMENTAL BOTANY, 69(19), 4609–4624. https://doi.org/10.1093/jxb/ery204
- Chicago author-date
- Vu, Lam Dai, Tingting Zhu, Inge Verstraeten, Brigitte Van De Cotte, Kris Gevaert, and Ive De Smet. 2018. “Temperature-Induced Changes in the Wheat Phosphoproteome Reveal Temperature-Regulated Interconversion of Phosphoforms.” JOURNAL OF EXPERIMENTAL BOTANY 69 (19): 4609–24. https://doi.org/10.1093/jxb/ery204.
- Chicago author-date (all authors)
- Vu, Lam Dai, Tingting Zhu, Inge Verstraeten, Brigitte Van De Cotte, Kris Gevaert, and Ive De Smet. 2018. “Temperature-Induced Changes in the Wheat Phosphoproteome Reveal Temperature-Regulated Interconversion of Phosphoforms.” JOURNAL OF EXPERIMENTAL BOTANY 69 (19): 4609–4624. doi:10.1093/jxb/ery204.
- Vancouver
- 1.Vu LD, Zhu T, Verstraeten I, Van De Cotte B, Gevaert K, De Smet I. Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms. JOURNAL OF EXPERIMENTAL BOTANY. 2018;69(19):4609–24.
- IEEE
- [1]L. D. Vu, T. Zhu, I. Verstraeten, B. Van De Cotte, K. Gevaert, and I. De Smet, “Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms,” JOURNAL OF EXPERIMENTAL BOTANY, vol. 69, no. 19, pp. 4609–4624, 2018.
@article{8575894, abstract = {{Wheat (Triticum ssp.) is one of the most important human food sources. However, this crop is very sensitive to temperature changes. Specifically, processes during wheat leaf, flower, and seed development and photosynthesis, which all contribute to the yield of this crop, are affected by high temperature. While this has to some extent been investigated on physiological, developmental, and molecular levels, very little is known about early signalling events associated with an increase in temperature. Phosphorylation-mediated signalling mechanisms, which are quick and dynamic, are associated with plant growth and development, also under abiotic stress conditions. Therefore, we probed the impact of a short-term and mild increase in temperature on the wheat leaf and spikelet phosphoproteome. In total, 3822 (containing 5178 phosphosites) and 5581 phosphopeptides (containing 7023 phosphosites) were identified in leaf and spikelet samples, respectively. Following statistical analysis, the resulting data set provides the scientific community with a first large-scale plant phosphoproteome under the control of higher ambient temperature. This community resource on the high temperature-mediated wheat phosphoproteome will be valuable for future studies. Our analyses also revealed a core set of common proteins between leaf and spikelet, suggesting some level of conserved regulatory mechanisms. Furthermore, we observed temperature-regulated interconversion of phosphoforms, which probably impacts protein activity.}}, author = {{Vu, Lam Dai and Zhu, Tingting and Verstraeten, Inge and Van De Cotte, Brigitte and Gevaert, Kris and De Smet, Ive}}, issn = {{0022-0957}}, journal = {{JOURNAL OF EXPERIMENTAL BOTANY}}, keywords = {{TRITICUM-AESTIVUM L.,HEAT-STRESS,PROTEIN-PHOSPHORYLATION,MOLECULAR-MECHANISMS,ABIOTIC STRESS,REPRODUCTIVE DEVELOPMENT,ARABIDOPSIS-THALIANA,RESPONSIVE PROTEINS,FREEZING TOLERANCE,PROTEOMIC,ANALYSIS,Leaf,phosphoproteomics,phosphorylation,signalling,spikelet,temperature,wheat}}, language = {{eng}}, number = {{19}}, pages = {{4609--4624}}, title = {{Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms}}, url = {{http://doi.org/10.1093/jxb/ery204}}, volume = {{69}}, year = {{2018}}, }
- Altmetric
- View in Altmetric
- Web of Science
- Times cited: