Sumoylation and phosphorylation: hidden and overt links
- Author(s)
- Konstantin Tomanov, Ella Nukarinen, Jorge Vicente, Guillermina M. Mendiondo, Nikola Winter, Lilian Nehlin, Wolfram Weckwerth, Michael J. Holdsworth, Markus Teige, Andreas Bachmair
- Abstract
Post-translational modifications are essential mediators between stimuli from development or the environment and adaptive transcriptional patterns. Recent data allow a first glimpse at how two modifications, phosphorylation and sumoylation, act interdependently to modulate stress responses. In particular, many components of the SUMO conjugation system are phosphoproteins, and some regulators and enzymes of protein phosphorylation can be sumoylated. Equally important, however, a number of proteins can be subject to both modifications. These substrates also have the capacity to connect stimuli transmitted via sumoylation with those transmitted via phosphorylation. As a prime example, we review data suggesting that nitrate reductase is a hub that integrates cues from these two modifications. Powerful proteomics approaches allowed the identification of additional common substrates, paving the way for studies to understand, on a broader basis, the cross-talk of phosphorylation with sumoylation and how it contributes to plant growth.
- Organisation(s)
- Department of Biochemistry and Cell Biology, Research Platform Vienna Metabolomics Center
- External organisation(s)
- University of Nottingham, Max F. Perutz Laboratories GmbH (MFPL)
- Journal
- Journal of Experimental Botany
- Volume
- 69
- Pages
- 4583-4590
- No. of pages
- 8
- ISSN
- 0022-0957
- DOI
- https://doi.org/10.1093/jxb/ery167
- Publication date
- 08-2018
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 106002 Biochemistry, 106037 Proteomics, 106052 Cell biology
- Keywords
- ASJC Scopus subject areas
- Physiology, Plant Science
- Portal url
- https://ucris.univie.ac.at/portal/en/publications/sumoylation-and-phosphorylation-hidden-and-overt-links(0a431e98-bfac-48b1-af55-6e0acce641b4).html