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Tripartite Motif-containing 33 (TRIM33) protein functions in the poly(ADP-ribose) polymerase (PARP)-dependent DNA damage response through interaction with Amplified in Liver Cancer 1 (ALC1) protein

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dc.contributor.authorKulkarni, Atul
dc.contributor.authorOza, Jay
dc.contributor.authorYao, Ming
dc.contributor.authorSohail, Honeah
dc.contributor.authorGinjala, Vasudeva
dc.contributor.authorTomas-Loba, Antonia
dc.contributor.authorHorejsi, Zuzana
dc.contributor.authorTan, Antoinette R
dc.contributor.authorBoulton, Simon J
dc.contributor.authorGanesan, Shridar
dc.contributor.departmentFisiología
dc.date.accessioned2024-02-09T07:48:15Z
dc.date.available2024-02-09T07:48:15Z
dc.date.issued2013-11-08
dc.description©<2013>. This manuscript version is made available under the CC-BY license http://creativecommons.org/licenses/by/4.0/ This document is the Published, version of a Published Work that appeared in final form in [Journal of Biological Chemistry]. To access the final edited and published work see [https://doi.org/10.1074/jbc.M113.459164]
dc.description.abstractActivation of poly(ADP-ribose) polymerase (PARP) near sites of DNA breaks facilitates recruitment of DNA repair proteins and promotes chromatin relaxation in part through the action of chromatin-remodeling enzyme Amplified in Liver Cancer 1 (ALC1). Through proteomic analysis we find that ALC1 interacts after DNA damage with Tripartite Motif-containing 33 (TRIM33), a multifunctional protein implicated in transcriptional regulation, TGF-β signaling, and tumorigenesis. We demonstrate that TRIM33 is dynamically recruited to DNA damage sites in a PARP1- and ALC1-dependent manner. TRIM33-deficient cells show enhanced sensitivity to DNA damage and prolonged retention of ALC1 at sites of DNA breaks. Conversely, overexpression of TRIM33 alleviates the DNA repair defects conferred by ALC1 overexpression. Thus, TRIM33 plays a role in PARP-dependent DNA damage response and regulates ALC1 activity by promoting its timely removal from sites of DNA damage.es
dc.formatapplication/pdfes
dc.format.extent13es
dc.identifier.doihttps://doi.org/10.1074/jbc.M113.459164
dc.identifier.eisbnJournal of Biological Chemistry, Vol. 288, Nº 45, 2013, pp. 32357–32369
dc.identifier.issnPrint: 0021-9258
dc.identifier.issnElectrónico: 1083-351X
dc.identifier.urihttp://hdl.handle.net/10201/139025
dc.languageenges
dc.publisherAmerican Society for Biochemistry and Molecular Biology [Society Publisher]es
dc.publisherElsevier
dc.relationNational Cancer Institute P30CA072720 NCIes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectALC1es
dc.subjectATPases
dc.subjectCancer biology
dc.subjectCell signaling
dc.subjectChromatin
dc.subjectDNA damage response
dc.subjectPARP
dc.subjectTRIM33
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Ciencias biológicas en general:577 - 577 Bioquímica. Biología molecular. Biofísica
dc.titleTripartite Motif-containing 33 (TRIM33) protein functions in the poly(ADP-ribose) polymerase (PARP)-dependent DNA damage response through interaction with Amplified in Liver Cancer 1 (ALC1) proteines
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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