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Article: Choice of biological source material supersedes oxidative stress in its influence on DJ-1 in vivo interactions with Hsp90

TitleChoice of biological source material supersedes oxidative stress in its influence on DJ-1 in vivo interactions with Hsp90
Authors
Keywordsmass spectrometry
interactome
DJ-1
Hsp90
iTRAQ
tcTPC
Issue Date2011
Citation
Journal of Proteome Research, 2011, v. 10, n. 10, p. 4388-4404 How to Cite?
AbstractDJ-1 is a small but relatively abundant protein of unknown function that may undergo stress-dependent cellular translocation and has been implicated in both neurodegenerative diseases and cancer. As such, DJ-1 may be an excellent study object to elucidate the relative influence of the cellular context on its interactome and for exploring whether acute exposure to oxidative stressors alters its molecular environment. Using quantitative mass spectrometry, we conducted comparative DJ-1 interactome analyses from in vivo cross-linked brains or livers and from hydrogen peroxide-treated or naïve embryonic stem cells. The analysis identified a subset of glycolytic enzymes, heat shock proteins 70 and 90, and peroxiredoxins as interactors of DJ-1. Consistent with a role of DJ-1 in Hsp90 chaperone biology, we document destabilization of Hsp90 clients in DJ-1 knockout cells. We further demonstrate the existence of a C106 sulfinic acid modification within DJ-1 and thereby establish that this previously inferred modification also exists in vivo. Our data suggest that caution has to be exerted in interpreting interactome data obtained from a single biological source material and identify a role of DJ-1 as an oxidative stress sensor and partner of a molecular machinery notorious for its involvement in cell fate decisions. © 2011 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/292662
ISSN
2023 Impact Factor: 3.8
2023 SCImago Journal Rankings: 1.299
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKnobbe, Christiane B.-
dc.contributor.authorRevett, Timothy J.-
dc.contributor.authorBai, Yu-
dc.contributor.authorChow, Vinca-
dc.contributor.authorJeon, Amy Hye Won-
dc.contributor.authorBöhm, Christopher-
dc.contributor.authorEhsani, Sepehr-
dc.contributor.authorKislinger, Thomas-
dc.contributor.authorMount, Howard T.-
dc.contributor.authorMak, Tak W.-
dc.contributor.authorSt. George-Hyslop, Peter-
dc.contributor.authorSchmitt-Ulms, Gerold-
dc.date.accessioned2020-11-17T14:56:57Z-
dc.date.available2020-11-17T14:56:57Z-
dc.date.issued2011-
dc.identifier.citationJournal of Proteome Research, 2011, v. 10, n. 10, p. 4388-4404-
dc.identifier.issn1535-3893-
dc.identifier.urihttp://hdl.handle.net/10722/292662-
dc.description.abstractDJ-1 is a small but relatively abundant protein of unknown function that may undergo stress-dependent cellular translocation and has been implicated in both neurodegenerative diseases and cancer. As such, DJ-1 may be an excellent study object to elucidate the relative influence of the cellular context on its interactome and for exploring whether acute exposure to oxidative stressors alters its molecular environment. Using quantitative mass spectrometry, we conducted comparative DJ-1 interactome analyses from in vivo cross-linked brains or livers and from hydrogen peroxide-treated or naïve embryonic stem cells. The analysis identified a subset of glycolytic enzymes, heat shock proteins 70 and 90, and peroxiredoxins as interactors of DJ-1. Consistent with a role of DJ-1 in Hsp90 chaperone biology, we document destabilization of Hsp90 clients in DJ-1 knockout cells. We further demonstrate the existence of a C106 sulfinic acid modification within DJ-1 and thereby establish that this previously inferred modification also exists in vivo. Our data suggest that caution has to be exerted in interpreting interactome data obtained from a single biological source material and identify a role of DJ-1 as an oxidative stress sensor and partner of a molecular machinery notorious for its involvement in cell fate decisions. © 2011 American Chemical Society.-
dc.languageeng-
dc.relation.ispartofJournal of Proteome Research-
dc.subjectmass spectrometry-
dc.subjectinteractome-
dc.subjectDJ-1-
dc.subjectHsp90-
dc.subjectiTRAQ-
dc.subjecttcTPC-
dc.titleChoice of biological source material supersedes oxidative stress in its influence on DJ-1 in vivo interactions with Hsp90-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/pr200225c-
dc.identifier.pmid21819105-
dc.identifier.scopuseid_2-s2.0-80053896620-
dc.identifier.volume10-
dc.identifier.issue10-
dc.identifier.spage4388-
dc.identifier.epage4404-
dc.identifier.eissn1535-3907-
dc.identifier.isiWOS:000295602700004-
dc.identifier.issnl1535-3893-

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