Publication Information
Nukarinen et al., 2017
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Abstract
Plant J. 2017 Aug;91(3):505-517. doi: 10.1111/tpj.13575. Epub 2017 Jun 4.
Protein sumoylation and phosphorylation intersect in Arabidopsis signaling.
Nukarinen E(1), Tomanov K(2), Ziba I(2), Weckwerth W(1)(3), Bachmair A(2).
Author information:
(1)Department of Ecogenomics and Systems Biology, BZA, University of Vienna,
Vienna, Austria.
(2)Department of Biochemistry and Cell Biology, Center for Molecular Biology,
Max F. Perutz Laboratories, Vienna, Austria.
(3)Vienna Metabolomics Center, University of Vienna, A-1060, Vienna, Austria.
Conjugation of the small ubiquitin-related modifier (SUMO) to protein substrates
has an impact on stress responses and on development. We analyzed the proteome
and phosphoproteome of mutants in this pathway. The mutants chosen had defects
in SUMO ligase SIZ1, which catalyzes attachment of single SUMO moieties onto
substrates, and in ligases PIAL1 and PIAL2, which are known to form SUMO chains.
A total of 2657 proteins and 550 phosphopeptides were identified and quantified.
Approximately 40% of the proteins and 20% of the phosphopeptides showed
differences in abundance in at least one of the analyzed genotypes,
demonstrating the influence of SUMO conjugation on protein abundance and
phosphorylation. The data show that PIAL1 and PIAL2 are integral parts of the
SUMO conjugation system with an impact on stress response, and confirm the
involvement of SIZ1 in plant defense. We find a high abundance of predicted SUMO
attachment sites in phosphoproteins (70% versus 40% in the total proteome),
suggesting convergence of phosphorylation and sumoylation signals onto a set of
common targets.
© 2017 The Authors The Plant Journal © 2017 John Wiley & Sons Ltd and Society
for Experimental Biology.
DOI: 10.1111/tpj.13575
PMCID: PMC5518230
PMID: 28419593 [Indexed for MEDLINE]
