Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology
Identifieur interne : 003E59 ( Pmc/Curation ); précédent : 003E58; suivant : 003E60Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology
Auteurs : Revati Wani [États-Unis] ; Asako Nagata [États-Unis] ; Brion W. Murray [États-Unis]Source :
- Frontiers in Pharmacology [ 1663-9812 ] ; 2014.
Abstract
The perception of reactive oxygen species has evolved over the past decade from agents of cellular damage to secondary messengers which modify signaling proteins in physiology and the disease state (e.g., cancer). New protein targets of specific oxidation are rapidly being identified. One emerging class of redox modification occurs to the thiol side chain of cysteine residues which can produce multiple chemically distinct alterations to the protein (e.g., sulfenic/sulfinic/sulfonic acid, disulfides). These post-translational modifications (PTM) are shown to affect the protein structure and function. Because redox-sensitive proteins can traffic between subcellular compartments that have different redox environments, cysteine oxidation enables a spatio-temporal control to signaling. Understanding ramifications of these oxidative modifications to the functions of signaling proteins is crucial for understanding cellular regulation as well as for informed-drug discovery process. The effects of EGFR oxidation of Cys797 on inhibitor pharmacology are presented to illustrate the principle. Taken together, cysteine redox PTM can impact both cell biology and drug pharmacology.
Url:
DOI: 10.3389/fphar.2014.00224
PubMed: 25339904
PubMed Central: 4186267
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology</title><author><name sortKey="Wani, Revati" sort="Wani, Revati" uniqKey="Wani R" first="Revati" last="Wani">Revati Wani</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Oncology Research Unit, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author><author><name sortKey="Nagata, Asako" sort="Nagata, Asako" uniqKey="Nagata A" first="Asako" last="Nagata">Asako Nagata</name><affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Worldwide Medicinal Chemistry, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author><author><name sortKey="Murray, Brion W" sort="Murray, Brion W" uniqKey="Murray B" first="Brion W." last="Murray">Brion W. Murray</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Oncology Research Unit, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25339904</idno><idno type="pmc">4186267</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4186267</idno><idno type="RBID">PMC:4186267</idno><idno type="doi">10.3389/fphar.2014.00224</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">003E60</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">003E60</idno><idno type="wicri:Area/Pmc/Curation">003E59</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">003E59</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology</title><author><name sortKey="Wani, Revati" sort="Wani, Revati" uniqKey="Wani R" first="Revati" last="Wani">Revati Wani</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Oncology Research Unit, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author><author><name sortKey="Nagata, Asako" sort="Nagata, Asako" uniqKey="Nagata A" first="Asako" last="Nagata">Asako Nagata</name><affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Worldwide Medicinal Chemistry, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author><author><name sortKey="Murray, Brion W" sort="Murray, Brion W" uniqKey="Murray B" first="Brion W." last="Murray">Brion W. Murray</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Oncology Research Unit, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Gwinnett Sports Rehabilitation, Gwinnett Medical Center, 500 Medical Center Blvd, Suite 130, Lawrenceville</wicri:regionArea></affiliation></author></analytic><series><title level="j">Frontiers in Pharmacology</title><idno type="eISSN">1663-9812</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The perception of reactive oxygen species has evolved over the past decade from agents of cellular damage to secondary messengers which modify signaling proteins in physiology and the disease state (e.g., cancer). New protein targets of specific oxidation are rapidly being identified. One emerging class of redox modification occurs to the thiol side chain of cysteine residues which can produce multiple chemically distinct alterations to the protein (e.g., sulfenic/sulfinic/sulfonic acid, disulfides). These post-translational modifications (PTM) are shown to affect the protein structure and function. Because redox-sensitive proteins can traffic between subcellular compartments that have different redox environments, cysteine oxidation enables a spatio-temporal control to signaling. Understanding ramifications of these oxidative modifications to the functions of signaling proteins is crucial for understanding cellular regulation as well as for informed-drug discovery process. The effects of EGFR oxidation of Cys<sub>797</sub> on inhibitor pharmacology are presented to illustrate the principle. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Front Pharmacol</journal-id><journal-id journal-id-type="iso-abbrev">Front Pharmacol</journal-id><journal-id journal-id-type="publisher-id">Front. Pharmacol.</journal-id><journal-title-group><journal-title>Frontiers in Pharmacology</journal-title></journal-title-group><issn pub-type="epub">1663-9812</issn><publisher><publisher-name>Frontiers Media S.A.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25339904</article-id><article-id pub-id-type="pmc">4186267</article-id><article-id pub-id-type="doi">10.3389/fphar.2014.00224</article-id><article-categories><subj-group subj-group-type="heading"><subject>Pharmacology</subject><subj-group><subject>Perspective Article</subject></subj-group></subj-group></article-categories><title-group><article-title>Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Wani</surname><given-names>Revati</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><uri xlink:type="simple" xlink:href="http://community.frontiersin.org/people/u/148036"></uri></contrib><contrib contrib-type="author"><name><surname>Nagata</surname><given-names>Asako</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref><uri xlink:type="simple" xlink:href="http://community.frontiersin.org/people/u/185679"></uri></contrib><contrib contrib-type="author"><name><surname>Murray</surname><given-names>Brion W.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn002"><sup>*</sup></xref><uri xlink:type="simple" xlink:href="http://community.frontiersin.org/people/u/32427"></uri></contrib></contrib-group><aff id="aff1"><sup>1</sup><institution>Oncology Research Unit, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></aff><aff id="aff2"><sup>2</sup><institution>Worldwide Medicinal Chemistry, Pfizer Worldwide Research and Development</institution><country>San Diego, CA, USA</country></aff><author-notes><fn fn-type="edited-by"><p>Edited by: <italic>Maurizio Bifulco, University of Salerno, Italy</italic></p></fn><fn fn-type="edited-by"><p>Reviewed by: <italic>Rayudu Gopalakrishna, University of Southern California, USA; Simona Pisanti, University of Salerno, Italy</italic></p></fn><corresp id="fn002">*Correspondence: <italic>Brion W. Murray, Oncology Research Unit, Pfizer Worldwide Research and Development, 10646 Science Center Drive, San Diego, CA 92121, USA e-mail: <email xlink:type="simple">brion.murray@pfizer.com</email></italic></corresp><fn fn-type="other" id="fn001"><p>This article was submitted to Pharmacology of Anti-Cancer Drugs, a section of the journal Frontiers in Pharmacology.</p></fn></author-notes><pub-date pub-type="epub"><day>06</day><month>10</month><year>2014</year></pub-date><pub-date pub-type="collection"><year>2014</year></pub-date><volume>5</volume><elocation-id>224</elocation-id><history><date date-type="received"><day>08</day><month>7</month><year>2014</year></date><date date-type="accepted"><day>17</day><month>9</month><year>2014</year></date></history><permissions><copyright-statement>Copyright © 2014 Wani, Nagata and Murray.</copyright-statement><copyright-year>2014</copyright-year><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p> This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p></license></permissions><abstract><p>The perception of reactive oxygen species has evolved over the past decade from agents of cellular damage to secondary messengers which modify signaling proteins in physiology and the disease state (e.g., cancer). New protein targets of specific oxidation are rapidly being identified. One emerging class of redox modification occurs to the thiol side chain of cysteine residues which can produce multiple chemically distinct alterations to the protein (e.g., sulfenic/sulfinic/sulfonic acid, disulfides). These post-translational modifications (PTM) are shown to affect the protein structure and function. Because redox-sensitive proteins can traffic between subcellular compartments that have different redox environments, cysteine oxidation enables a spatio-temporal control to signaling. Understanding ramifications of these oxidative modifications to the functions of signaling proteins is crucial for understanding cellular regulation as well as for informed-drug discovery process. The effects of EGFR oxidation of Cys<sub>797</sub> on inhibitor pharmacology are presented to illustrate the principle. Taken together, cysteine redox PTM can impact both cell biology and drug pharmacology.</p></abstract><kwd-group><kwd>ROS</kwd><kwd>redox</kwd><kwd>cysteine oxidation</kwd><kwd>kinase</kwd><kwd>EGFR</kwd><kwd>subcellular trafficking</kwd><kwd>covalent drugs</kwd></kwd-group><counts><fig-count count="1"></fig-count><table-count count="1"></table-count><equation-count count="0"></equation-count><ref-count count="66"></ref-count><page-count count="8"></page-count><word-count count="0"></word-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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