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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, X2 1
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
2013 Impact Factor: 11.444
 
DOIhttp://dx.doi.org/10.1021/ja210528v
 
ReferencesReferences in Scopus
 
DC FieldValue
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.eissn1520-5126
 
dc.identifier.epage1985
 
dc.identifier.issn0002-7863
2013 Impact Factor: 11.444
 
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
 
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<contributor.author>Chait, BT</contributor.author>
<contributor.author>Kapoor, TM</contributor.author>
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Author Affiliations
  1. The University of Hong Kong
  2. Rockefeller University