Show simple item record

dc.contributor.authorPapachristou, Eva
dc.contributor.authorKishore, Kamal
dc.contributor.authorHolding, Andrew
dc.contributor.authorHarvey, Kate
dc.contributor.authorRoumeliotis, Theodoros I
dc.contributor.authorChilamakuri, Chandra
dc.contributor.authorOmarjee, Soleilmane
dc.contributor.authorChia, Kee Ming
dc.contributor.authorSwarbrick, Alex
dc.contributor.authorLim, Elgene
dc.contributor.authorMarkowetz, Florian
dc.contributor.authorEldridge, Matthew
dc.contributor.authorSiersbaek, Rasmus
dc.contributor.authorD'Santos, Clive S
dc.contributor.authorCarroll, Jason
dc.date.accessioned2018-09-26T13:00:14Z
dc.date.available2018-09-26T13:00:14Z
dc.date.issued2018-06-13
dc.identifier.issn2041-1723
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/280762
dc.description.abstractUnderstanding the dynamics of endogenous protein-protein interactions in complex networks is pivotal in deciphering disease mechanisms. To enable the in-depth analysis of protein interactions in chromatin-associated protein complexes, we have previously developed a method termed RIME (Rapid Immunoprecipitation Mass spectrometry of Endogenous proteins). Here, we present a quantitative multiplexed method (qPLEX-RIME), which integrates RIME with isobaric labelling and tribrid mass spectrometry for the study of protein interactome dynamics in a quantitative fashion with increased sensitivity. Using the qPLEX-RIME method, we delineate the temporal changes of the Estrogen Receptor alpha (ERα) interactome in breast cancer cells treated with 4-hydroxytamoxifen. Furthermore, we identify endogenous ERα-associated proteins in human Patient-Derived Xenograft tumours and in primary human breast cancer clinical tissue. Our results demonstrate that the combination of RIME with isobaric labelling offers a powerful tool for the in-depth and quantitative characterisation of protein interactome dynamics, which is applicable to clinical samples.
dc.languageeng
dc.publisherSpringer Nature
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBreast cancer
dc.subjectImmunoprecipitation
dc.subjectMass spectrometry
dc.subjectProtein–protein interaction networks
dc.titleA quantitative mass spectrometry-based approach to monitor the dynamics of endogenous chromatin-associated protein complexes.
dc.typeArticle
prism.endingPage2311
prism.issueIdentifier1
prism.number2311
prism.publicationDate2018
prism.publicationNameNature Communications
prism.startingPage2311
prism.volume9
dc.identifier.doi10.17863/CAM.28126
dcterms.dateAccepted2018-05-03
rioxxterms.versionofrecord10.1038/s41467-018-04619-5
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.licenseref.startdate2018-06-13
dc.contributor.orcidPapachristou, Eva [0000-0002-5835-2055]
dc.contributor.orcidKishore, Kamal [0000-0002-4650-8745]
dc.contributor.orcidHolding, Andrew [0000-0002-8459-7048]
dc.contributor.orcidMarkowetz, Florian [0000-0002-2784-5308]
dc.contributor.orcidEldridge, Matthew [0000-0002-5799-8911]
dc.contributor.orcidCarroll, Jason [0000-0003-3643-0080]
dc.identifier.eissn2041-1723
dc.publisher.urlhttps://www.nature.com/articles/s41467-018-04619-5#article-info
rioxxterms.typeJournal Article/Review
pubs.funder-project-idWellcome Trust (108467/Z/15/Z)
pubs.funder-project-idCancer Research UK (C14303/A17197)
pubs.funder-project-idBreast Cancer Campaign (2012NovemberPR042)
pubs.funder-project-idEuropean Research Council (646876)
pubs.funder-project-idCancer Research UK (CRUK-A19274)
cam.issuedOnline2018-06-13
dc.identifier.urlhttps://www.nature.com/articles/s41467-018-04619-5#article-info


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International