The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Large-Scale Arabidopsis Phosphoproteome Profiling Reveals Novel Chloroplast Kinase Substrates and Phosphorylation Networks
Open accessAbstract
We have characterized the phosphoproteome of Arabidopsis (Arabidopsis thaliana) seedlings using high-accuracy mass spectrometry and report the identification of 1,429 phosphoproteins and 3,029 unique phosphopeptides. Among these, 174 proteins were chloroplast phosphoproteins. Motif-X (motif extractor) analysis of the phosphorylation sites in chloroplast proteins identified four significantly enriched kinase motifs, which include casein kinase II (CKII) and proline-directed kinase motifs, as well as two new motifs at the carboxyl terminus of ribosomal proteins. Using the phosphorylation motifs as a footprint for the activity of a specific kinase class, we connected the phosphoproteins with their putative kinases and constructed a chloroplast CKII phosphorylation network. The network topology suggests that CKII is a central regulator of different chloroplast functions. To provide insights into the dynamic regulation of protein phosphorylation, we analyzed the phosphoproteome at the end of day and end of night. The results revealed only minor changes in chloroplast kinase activities and phosphorylation site utilization. A notable exception was ATP synthase β-subunit, which is found phosphorylated at CKII phosphorylation sites preferentially in the dark. We propose that ATP synthase is regulated in cooperation with 14-3-3 proteins by CKII-mediated phosphorylation of ATP synthase β-subunit in the dark.
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Cited by
Kosová, K., Vítámvás, P., Prášil, I. T., & Renaut, J. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.02.006 · Cited by 852
Signaling Toward Reactive Oxygen Species-Scavenging Enzymes in Plants
Dvořák, P., Krasylenko, Y., Zeiner, A., Šamaj, J., & Takáč, T. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2020.618835 · Cited by 375
Zou, J.-J., Li, X.-D., Ratnasekera, D., Wang, C., Liu, W.-X., Song, L.-F., Zhang, W.-Z., & Wu, W.-H. (2015) · The Plant Cell · doi:10.1105/tpc.15.00144 · Cited by 360
Regulation of starch biosynthesis in response to a fluctuating environment
Geigenberger, P. (2011) · Plant Physiology · doi:10.1104/pp.110.170399 · Cited by 348
Quantitation in Mass-Spectrometry-Based Proteomics
Schulze, W. X., & Usadel, B. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112132 · Cited by 344
Metadata
- Authors
- Reiland, S., Messerli, G., Baerenfaller, K., Gerrits, B., Endler, A., Grossmann, J., Gruissem, W., & Baginsky, S.
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-04-17
- Volume
- 150
- Issue
- 2
- Pages
- 889-903
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- OpenAlex
- W2139750884
- Cited by
- 481
- References
- 41
- FWCI
- 15.24
- Type
- journal article
- Language
- en
- Open access
- green
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- Reiland, S., Messerli, G., Baerenfaller, K., Gerrits, B., Endler, A., Grossmann, J., Gruissem, W., & Baginsky, S. (2009). Large-Scale Arabidopsis Phosphoproteome Profiling Reveals Novel Chloroplast Kinase Substrates and Phosphorylation Networks. Plant Physiology. https://doi.org/10.1104/pp.109.138677
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