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- Publisher Website: 10.1021/ja210528v
- Scopus: eid_2-s2.0-84863079871
- PMID: 22239320
- WOS: WOS:000301084600023
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Article: Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions
Title | Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions |
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Authors | |
Issue Date | 2012 |
Publisher | American 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 Identifier | http://hdl.handle.net/10722/168641 |
ISSN | 2021 Impact Factor: 16.383 2020 SCImago Journal Rankings: 7.115 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Li, X | en_US |
dc.contributor.author | Foley, EA | en_US |
dc.contributor.author | Molloy, KR | en_US |
dc.contributor.author | Li, Y | en_US |
dc.contributor.author | Chait, BT | en_US |
dc.contributor.author | Kapoor, TM | en_US |
dc.date.accessioned | 2012-10-08T03:23:50Z | - |
dc.date.available | 2012-10-08T03:23:50Z | - |
dc.date.issued | 2012 | en_US |
dc.identifier.citation | Journal Of The American Chemical Society, 2012, v. 134 n. 4, p. 1982-1985 | en_US |
dc.identifier.issn | 0002-7863 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/168641 | - |
dc.description.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. | en_US |
dc.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html | en_US |
dc.relation.ispartof | Journal of the American Chemical Society | en_US |
dc.subject.mesh | Cells, Cultured | en_US |
dc.subject.mesh | Hela Cells | en_US |
dc.subject.mesh | Histones - Chemistry - Metabolism | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Lysine - Chemistry - Metabolism | en_US |
dc.subject.mesh | Mass Spectrometry | en_US |
dc.subject.mesh | Molecular Structure | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Protein Processing, Post-Translational | en_US |
dc.subject.mesh | Proteins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Proteomics | en_US |
dc.title | Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions | en_US |
dc.type | Article | en_US |
dc.identifier.email | Li, X:xiangli@hku.hk | en_US |
dc.identifier.authority | Li, X=rp01562 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1021/ja210528v | en_US |
dc.identifier.pmid | 22239320 | - |
dc.identifier.pmcid | PMC3520067 | - |
dc.identifier.scopus | eid_2-s2.0-84863079871 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-84863079871&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 134 | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.spage | 1982 | en_US |
dc.identifier.epage | 1985 | en_US |
dc.identifier.eissn | 1520-5126 | - |
dc.identifier.isi | WOS:000301084600023 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Li, X=49761544200 | en_US |
dc.identifier.scopusauthorid | Foley, EA=24399005100 | en_US |
dc.identifier.scopusauthorid | Molloy, KR=36243859800 | en_US |
dc.identifier.scopusauthorid | Li, Y=24830565600 | en_US |
dc.identifier.scopusauthorid | Chait, BT=54940930600 | en_US |
dc.identifier.scopusauthorid | Kapoor, TM=7003935028 | en_US |
dc.identifier.citeulike | 10364834 | - |
dc.identifier.issnl | 0002-7863 | - |