Premium
Protein sumoylation and phosphorylation intersect in Arabidopsis signaling
Author(s) -
Nukarinen Ella,
Tomanov Konstantin,
Ziba Ionida,
Weckwerth Wolfram,
Bachmair Andreas
Publication year - 2017
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13575
Subject(s) - sumo protein , phosphorylation , biology , proteome , sumo enzymes , ubiquitin ligase , mutant , ubiquitin , biochemistry , proteomics , arabidopsis , microbiology and biotechnology , signal transduction , gene
Summary 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 SIZ 1, which catalyzes attachment of single SUMO moieties onto substrates, and in ligases PIAL 1 and PIAL 2, 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 PIAL 1 and PIAL 2 are integral parts of the SUMO conjugation system with an impact on stress response, and confirm the involvement of SIZ 1 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.