Title | Mining for protein S-sulfenylation in uncovers redox-sensitive sites. |
Publication Type | Journal Article |
Year of Publication | 2019 |
Authors | Huang, J., P. Willems, B. Wei, C. Tian, R. B. Ferreira, N. Bodra, S. AgustÃn M. Gache, K. Wahni, K. Liu, D. Vertommen, K. Gevaert, K. S. Carroll, M. Van Montagu, J. Yang, F. Van Breusegem, and J. Messens |
Journal | Proc Natl Acad Sci U S A |
Volume | 116 |
Issue | 42 |
Pagination | 21256-21261 |
Date Published | 2019 Oct 15 |
ISSN | 1091-6490 |
Abstract | Hydrogen peroxide (HO) is an important messenger molecule for diverse cellular processes. HO oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we mapped 1,537 S-sulfenylated sites on more than 1,000 proteins in cells. Proteins involved in RNA homeostasis and metabolism were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located at catalytic sites of enzymes or on cysteines involved in metal binding, hinting at a direct mode of action for redox regulation. Comparison of human and S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which has been identified previously as being S-sulfenylated. We show that, by replacing Cys181 of recombinant AtMAPK4 by a redox-insensitive serine residue, the kinase activity decreased, indicating the importance of this noncatalytic cysteine for the kinase mechanism. Altogether, we quantitatively mapped the S-sulfenylated cysteines in cells under HO stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies. |
DOI | 10.1073/pnas.1906768116 |
Alternate Journal | Proc. Natl. Acad. Sci. U.S.A. |
PubMed ID | 31578252 |
PubMed Central ID | PMC6800386 |
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