Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites.
Identifieur interne : 000018 ( Main/Corpus ); précédent : 000017; suivant : 000019Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites.
Auteurs : Jingjing Huang ; Patrick Willems ; Bo Wei ; Caiping Tian ; Renan B. Ferreira ; Nandita Bodra ; Santiago Agustín Martínez Gache ; Khadija Wahni ; Keke Liu ; Didier Vertommen ; Kris Gevaert ; Kate S. Carroll ; Marc Van Montagu ; Jing Yang ; Frank Van Breusegem ; Joris MessensSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2019.
English descriptors
- KwdEn :
- Arabidopsis (metabolism), Catalytic Domain (physiology), Cysteine (metabolism), Humans (MeSH), Hydrogen Peroxide (metabolism), Mitogen-Activated Protein Kinase 1 (metabolism), Oxidation-Reduction (MeSH), Proteins (metabolism), RNA (metabolism), Serine (metabolism), Signal Transduction (physiology), Sulfenic Acids (metabolism), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , metabolism : Cysteine, Hydrogen Peroxide, Mitogen-Activated Protein Kinase 1, Proteins, RNA, Serine, Sulfenic Acids, Sulfhydryl Compounds.
- metabolism : Arabidopsis.
- physiology : Catalytic Domain, Signal Transduction.
- Humans, Oxidation-Reduction.
Abstract
Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 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 Arabidopsis thaliana 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 Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis 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 Arabidopsis cells under H2O2 stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.
DOI: 10.1073/pnas.1906768116
PubMed: 31578252
PubMed Central: PMC6800386
Links to Exploration step
pubmed:31578252Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mining for protein S-sulfenylation in <i>Arabidopsis</i> uncovers redox-sensitive sites.</title><author><name sortKey="Huang, Jingjing" sort="Huang, Jingjing" uniqKey="Huang J" first="Jingjing" last="Huang">Jingjing Huang</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Willems, Patrick" sort="Willems, Patrick" uniqKey="Willems P" first="Patrick" last="Willems">Patrick Willems</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Wei, Bo" sort="Wei, Bo" uniqKey="Wei B" first="Bo" last="Wei">Bo Wei</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Tian, Caiping" sort="Tian, Caiping" uniqKey="Tian C" first="Caiping" last="Tian">Caiping Tian</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Ferreira, Renan B" sort="Ferreira, Renan B" uniqKey="Ferreira R" first="Renan B" last="Ferreira">Renan B. Ferreira</name><affiliation><nlm:affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</nlm:affiliation></affiliation></author><author><name sortKey="Bodra, Nandita" sort="Bodra, Nandita" uniqKey="Bodra N" first="Nandita" last="Bodra">Nandita Bodra</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Martinez Gache, Santiago Agustin" sort="Martinez Gache, Santiago Agustin" uniqKey="Martinez Gache S" first="Santiago Agustín" last="Martínez Gache">Santiago Agustín Martínez Gache</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Wahni, Khadija" sort="Wahni, Khadija" uniqKey="Wahni K" first="Khadija" last="Wahni">Khadija Wahni</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Keke" sort="Liu, Keke" uniqKey="Liu K" first="Keke" last="Liu">Keke Liu</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Vertommen, Didier" sort="Vertommen, Didier" uniqKey="Vertommen D" first="Didier" last="Vertommen">Didier Vertommen</name><affiliation><nlm:affiliation>de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Gevaert, Kris" sort="Gevaert, Kris" uniqKey="Gevaert K" first="Kris" last="Gevaert">Kris Gevaert</name><affiliation><nlm:affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Carroll, Kate S" sort="Carroll, Kate S" uniqKey="Carroll K" first="Kate S" last="Carroll">Kate S. Carroll</name><affiliation><nlm:affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</nlm:affiliation></affiliation></author><author><name sortKey="Van Montagu, Marc" sort="Van Montagu, Marc" uniqKey="Van Montagu M" first="Marc" last="Van Montagu">Marc Van Montagu</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Jing" sort="Yang, Jing" uniqKey="Yang J" first="Jing" last="Yang">Jing Yang</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation></author><author><name sortKey="Van Breusegem, Frank" sort="Van Breusegem, Frank" uniqKey="Van Breusegem F" first="Frank" last="Van Breusegem">Frank Van Breusegem</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Messens, Joris" sort="Messens, Joris" uniqKey="Messens J" first="Joris" last="Messens">Joris Messens</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:31578252</idno><idno type="pmid">31578252</idno><idno type="doi">10.1073/pnas.1906768116</idno><idno type="pmc">PMC6800386</idno><idno type="wicri:Area/Main/Corpus">000018</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000018</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mining for protein S-sulfenylation in <i>Arabidopsis</i> uncovers redox-sensitive sites.</title><author><name sortKey="Huang, Jingjing" sort="Huang, Jingjing" uniqKey="Huang J" first="Jingjing" last="Huang">Jingjing Huang</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Willems, Patrick" sort="Willems, Patrick" uniqKey="Willems P" first="Patrick" last="Willems">Patrick Willems</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Wei, Bo" sort="Wei, Bo" uniqKey="Wei B" first="Bo" last="Wei">Bo Wei</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Tian, Caiping" sort="Tian, Caiping" uniqKey="Tian C" first="Caiping" last="Tian">Caiping Tian</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Ferreira, Renan B" sort="Ferreira, Renan B" uniqKey="Ferreira R" first="Renan B" last="Ferreira">Renan B. Ferreira</name><affiliation><nlm:affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</nlm:affiliation></affiliation></author><author><name sortKey="Bodra, Nandita" sort="Bodra, Nandita" uniqKey="Bodra N" first="Nandita" last="Bodra">Nandita Bodra</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Martinez Gache, Santiago Agustin" sort="Martinez Gache, Santiago Agustin" uniqKey="Martinez Gache S" first="Santiago Agustín" last="Martínez Gache">Santiago Agustín Martínez Gache</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Wahni, Khadija" sort="Wahni, Khadija" uniqKey="Wahni K" first="Khadija" last="Wahni">Khadija Wahni</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Keke" sort="Liu, Keke" uniqKey="Liu K" first="Keke" last="Liu">Keke Liu</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Vertommen, Didier" sort="Vertommen, Didier" uniqKey="Vertommen D" first="Didier" last="Vertommen">Didier Vertommen</name><affiliation><nlm:affiliation>de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Gevaert, Kris" sort="Gevaert, Kris" uniqKey="Gevaert K" first="Kris" last="Gevaert">Kris Gevaert</name><affiliation><nlm:affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Carroll, Kate S" sort="Carroll, Kate S" uniqKey="Carroll K" first="Kate S" last="Carroll">Kate S. Carroll</name><affiliation><nlm:affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</nlm:affiliation></affiliation></author><author><name sortKey="Van Montagu, Marc" sort="Van Montagu, Marc" uniqKey="Van Montagu M" first="Marc" last="Van Montagu">Marc Van Montagu</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Jing" sort="Yang, Jing" uniqKey="Yang J" first="Jing" last="Yang">Jing Yang</name><affiliation><nlm:affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation></author><author><name sortKey="Van Breusegem, Frank" sort="Van Breusegem, Frank" uniqKey="Van Breusegem F" first="Frank" last="Van Breusegem">Frank Van Breusegem</name><affiliation><nlm:affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Messens, Joris" sort="Messens, Joris" uniqKey="Messens J" first="Joris" last="Messens">Joris Messens</name><affiliation><nlm:affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (metabolism)</term><term>Catalytic Domain (physiology)</term><term>Cysteine (metabolism)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (metabolism)</term><term>Mitogen-Activated Protein Kinase 1 (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Proteins (metabolism)</term><term>RNA (metabolism)</term><term>Serine (metabolism)</term><term>Signal Transduction (physiology)</term><term>Sulfenic Acids (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Hydrogen Peroxide</term><term>Mitogen-Activated Protein Kinase 1</term><term>Proteins</term><term>RNA</term><term>Serine</term><term>Sulfenic Acids</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Catalytic Domain</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Oxidation-Reduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) is an important messenger molecule for diverse cellular processes. H<sub>2</sub>O<sub>2</sub> 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 <i>Arabidopsis thaliana</i> 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 <i>Arabidopsis</i> S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the <i>Arabidopsis</i> 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 <i>Arabidopsis</i> cells under H<sub>2</sub>O<sub>2</sub> stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31578252</PMID><DateCompleted><Year>2020</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>116</Volume><Issue>42</Issue><PubDate><Year>2019</Year><Month>10</Month><Day>15</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Mining for protein S-sulfenylation in <i>Arabidopsis</i> uncovers redox-sensitive sites.</ArticleTitle><Pagination><MedlinePgn>21256-21261</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1906768116</ELocationID><Abstract><AbstractText>Hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) is an important messenger molecule for diverse cellular processes. H<sub>2</sub>O<sub>2</sub> 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 <i>Arabidopsis thaliana</i> 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 <i>Arabidopsis</i> S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the <i>Arabidopsis</i> 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 <i>Arabidopsis</i> cells under H<sub>2</sub>O<sub>2</sub> stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Jingjing</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Willems</LastName><ForeName>Patrick</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wei</LastName><ForeName>Bo</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tian</LastName><ForeName>Caiping</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferreira</LastName><ForeName>Renan B</ForeName><Initials>RB</Initials><AffiliationInfo><Affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bodra</LastName><ForeName>Nandita</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martínez Gache</LastName><ForeName>Santiago Agustín</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wahni</LastName><ForeName>Khadija</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Keke</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vertommen</LastName><ForeName>Didier</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gevaert</LastName><ForeName>Kris</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carroll</LastName><ForeName>Kate S</ForeName><Initials>KS</Initials><AffiliationInfo><Affiliation>Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Van Montagu</LastName><ForeName>Marc</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0003-4711-5131</Identifier><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Jing</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0001-8486-273X</Identifier><AffiliationInfo><Affiliation>State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences, Beijing Institute of Lifeomics, 102206 Beijing, China; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Van Breusegem</LastName><ForeName>Frank</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Plant Systems Biology, VIB, 9052 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Messens</LastName><ForeName>Joris</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-2128-8264</Identifier><AffiliationInfo><Affiliation>Center for Structural Biology, VIB, 1050 Brussels, Belgium; marc.vanmontagu@ugent.be yangjing54@hotmail.com frank.vanbreusegem@psb.vib-ugent.be joris.messens@vub.vib.be.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Brussels Center for Redox Biology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA227849</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM087638</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM102187</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>10</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013434">Sulfenic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>452VLY9402</RegistryNumber><NameOfSubstance UI="D012694">Serine</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber><NameOfSubstance UI="D019950">Mitogen-Activated Protein Kinase 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019950" MajorTopicYN="N">Mitogen-Activated Protein Kinase 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013434" MajorTopicYN="N">Sulfenic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Arabidopsis</Keyword><Keyword MajorTopicYN="Y">S-sulfenylation</Keyword><Keyword MajorTopicYN="Y">chemoproteomics</Keyword><Keyword MajorTopicYN="Y">posttranslational modification</Keyword><Keyword MajorTopicYN="Y">redox regulation</Keyword></KeywordList><CoiStatement>The authors declare no competing interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>10</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>10</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31578252</ArticleId><ArticleId IdType="pii">1906768116</ArticleId><ArticleId IdType="doi">10.1073/pnas.1906768116</ArticleId><ArticleId IdType="pmc">PMC6800386</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Plant Cell. 2007 Oct;19(10):3266-79</Citation><ArticleIdList><ArticleId 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