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, Department of Ecogenomics and Systems Biology, Large-Instrument Facility for Mass Spectrometry in Life Sciences, Research Platform Vienna Metabolomics Center
Journal
Journal of Experimental Botany
Volume
69
Pages
4583-4590
ISSN
0022-0957
DOI
https://doi.org/10.1093/jxb/ery167
Publication date
05-2018
Publication status
Published
Peer reviewed
Yes
Austrian Fields of Science 2012
106002 Biochemistry, 106052 Cell biology, 106037 Proteomics
Keywords
Nitrate reductase, phytochrome B, protein modification, protein phosphorylation, SUMO
Portal url
https://ucris.univie.ac.at/portal/en/publications/sumoylation-and-phosphorylation-hidden-and-overt-links(0a431e98-bfac-48b1-af55-6e0acce641b4).html