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

TitleQuantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions
Authors
Issue Date2012
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2012, v. 134 n. 4, p. 1982-1985 How to Cite?
Abstract
Post-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.
Persistent Identifierhttp://hdl.handle.net/10722/168641
ISSN
2013 Impact Factor: 11.444
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong
  2. Rockefeller University
DC FieldValueLanguage
dc.contributor.authorLi, Xen_US
dc.contributor.authorFoley, EAen_US
dc.contributor.authorMolloy, KRen_US
dc.contributor.authorLi, Yen_US
dc.contributor.authorChait, BTen_US
dc.contributor.authorKapoor, TMen_US
dc.date.accessioned2012-10-08T03:23:50Z-
dc.date.available2012-10-08T03:23:50Z-
dc.date.issued2012en_US
dc.identifier.citationJournal Of The American Chemical Society, 2012, v. 134 n. 4, p. 1982-1985en_US
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://hdl.handle.net/10722/168641-
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.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_US
dc.relation.ispartofJournal of the American Chemical Societyen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHistones - Chemistry - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshLysine - Chemistry - Metabolismen_US
dc.subject.meshMass Spectrometryen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshProteins - Chemistry - Metabolismen_US
dc.subject.meshProteomicsen_US
dc.titleQuantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactionsen_US
dc.typeArticleen_US
dc.identifier.emailLi, X:xiangli@hku.hken_US
dc.identifier.authorityLi, X=rp01562en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja210528ven_US
dc.identifier.pmid22239320en_US
dc.identifier.scopuseid_2-s2.0-84863079871en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84863079871&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume134en_US
dc.identifier.issue4en_US
dc.identifier.spage1982en_US
dc.identifier.epage1985en_US
dc.identifier.eissn1520-5126-
dc.identifier.isiWOS:000301084600023-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLi, X=49761544200en_US
dc.identifier.scopusauthoridFoley, EA=24399005100en_US
dc.identifier.scopusauthoridMolloy, KR=36243859800en_US
dc.identifier.scopusauthoridLi, Y=24830565600en_US
dc.identifier.scopusauthoridChait, BT=54940930600en_US
dc.identifier.scopusauthoridKapoor, TM=7003935028en_US
dc.identifier.citeulike10364834-

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