Article: Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions

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TitleQuantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions
AuthorsLi, X1 2
Foley, EA2
Molloy, KR2
Li, Y2
Chait, BT2
Kapoor, TM2
Issue Date2012
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
CitationJournal Of The American Chemical Society, 2012, v. 134 n. 4, p. 1982-1985 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja210528v
AbstractPost-translational modifications (PTMs) (e.g., acetylation, methylation, and phosphorylation) play crucial roles in regulating the diverse protein-protein interactions involved in essentially every cellular process. While significant progress has been made to detect PTMs, profiling protein-protein interactions mediated by these PTMs remains a challenge. Here, we report a method that combines a photo-cross-linking strategy with stable isotope labeling in cell culture (SILAC)-based quantitative mass spectrometry to identify PTM-dependent protein-protein interactions. To develop and apply this approach, we focused on trimethylated lysine-4 at the histone H3 N-terminus (H3K4Me 3), a PTM linked to actively transcribed gene promoters. Our approach identified proteins previously known to recognize this modification and MORC3 as a new protein that binds H3M4Me 3. This study indicates that our cross-linking-assisted and SILAC-based protein identification (CLASPI) approach can be used to profile protein-protein interactions mediated by PTMs, such as lysine methylation. © 2012 American Chemical Society.
ISSN0002-7863
2011 Impact Factor: 9.907
2011 SCImago Journal Rankings: 1.117
DOIhttp://dx.doi.org/10.1021/ja210528v
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorLi, X
dc.contributor.authorFoley, EA
dc.contributor.authorMolloy, KR
dc.contributor.authorLi, Y
dc.contributor.authorChait, BT
dc.contributor.authorKapoor, TM
dc.date.accessioned2012-10-08T03:23:50Z
dc.date.available2012-10-08T03:23:50Z
dc.date.issued2012
dc.description.abstractPost-translational modifications (PTMs) (e.g., acetylation, methylation, and phosphorylation) play crucial roles in regulating the diverse protein-protein interactions involved in essentially every cellular process. While significant progress has been made to detect PTMs, profiling protein-protein interactions mediated by these PTMs remains a challenge. Here, we report a method that combines a photo-cross-linking strategy with stable isotope labeling in cell culture (SILAC)-based quantitative mass spectrometry to identify PTM-dependent protein-protein interactions. To develop and apply this approach, we focused on trimethylated lysine-4 at the histone H3 N-terminus (H3K4Me 3), a PTM linked to actively transcribed gene promoters. Our approach identified proteins previously known to recognize this modification and MORC3 as a new protein that binds H3M4Me 3. This study indicates that our cross-linking-assisted and SILAC-based protein identification (CLASPI) approach can be used to profile protein-protein interactions mediated by PTMs, such as lysine methylation. © 2012 American Chemical Society.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal Of The American Chemical Society, 2012, v. 134 n. 4, p. 1982-1985 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja210528v
dc.identifier.citeulike10364834
dc.identifier.doihttp://dx.doi.org/10.1021/ja210528v
dc.identifier.epage1985
dc.identifier.issn0002-7863
2011 Impact Factor: 9.907
2011 SCImago Journal Rankings: 1.117
dc.identifier.issue4
dc.identifier.pmid22239320
dc.identifier.scopuseid_2-s2.0-84863079871
dc.identifier.spage1982
dc.identifier.urihttp://hdl.handle.net/10722/168641
dc.identifier.volume134
dc.languageeng
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
dc.publisher.placeUnited States
dc.relation.ispartofJournal of the American Chemical Society
dc.relation.referencesReferences in Scopus
dc.subject.meshCells, Cultured
dc.subject.meshHela Cells
dc.subject.meshHistones - Chemistry - Metabolism
dc.subject.meshHumans
dc.subject.meshLysine - Chemistry - Metabolism
dc.subject.meshMass Spectrometry
dc.subject.meshMolecular Structure
dc.subject.meshProtein Binding
dc.subject.meshProtein Processing, Post-Translational
dc.subject.meshProteins - Chemistry - Metabolism
dc.subject.meshProteomics
dc.titleQuantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong
  2. Rockefeller University