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dc.contributor.authorAlm-Kristiansen, Anne H
dc.contributor.authorLorenzo, Petra I
dc.contributor.authorMolværsmyr, Ann-Kristin
dc.contributor.authorMatre, Vilborg
dc.contributor.authorLedsaak, Marit
dc.contributor.authorSæther, Thomas
dc.contributor.authorGabrielsen, Odd S
dc.date.accessioned2015-10-09T01:16:41Z
dc.date.available2015-10-09T01:16:41Z
dc.date.issued2011
dc.identifier.citationMolecular Cancer. 2011 Feb 21;10(1):21
dc.identifier.urihttp://hdl.handle.net/10852/46459
dc.description.abstractBackground FLASH is a huge nuclear protein involved in various cellular functions such as apoptosis signalling, NF-κB activation, S-phase regulation, processing of histone pre-mRNAs, and co-regulation of transcription. Recently, we identified FLASH as a co-activator of the transcription factor c-Myb and found FLASH to be tightly associated with active transcription foci. As a huge multifunctional protein, FLASH is expected to have many interaction partners, some which may shed light on its function as a transcriptional regulator. Results To find additional FLASH-associated proteins, we performed a yeast two-hybrid (Y2H) screening with FLASH as bait and identified the SUMO E3 ligase PIAS1 as an interaction partner. The association appears to involve two distinct interaction surfaces in FLASH. We verified the interaction by Y2H-mating, GST pulldowns, co-IP and ChIP. FLASH and PIAS1 were found to co-localize in nuclear speckles. Functional assays revealed that PIAS1 enhances the intrinsic transcriptional activity of FLASH in a RING finger-dependent manner. Furthermore, PIAS1 also augments the specific activity of c-Myb, and cooperates with FLASH to further co-activate c-Myb. The three proteins, FLASH, PIAS1, and c-Myb, are all co-localized with active RNA polymerase II foci, resembling transcription factories. Conclusions We conclude that PIAS1 is a common partner for two cancer-related nuclear factors, c-Myb and FLASH. Our results point to a functional cooperation between FLASH and PIAS1 in the enhancement of c-Myb activity in active nuclear foci.
dc.language.isoeng
dc.rightsAlm-Kristiansen et al; licensee BioMed Central Ltd.
dc.rightsAttribution 2.0 Generic
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/
dc.titlePIAS1 interacts with FLASH and enhances its co-activation of c-Myb
dc.typeJournal article
dc.date.updated2015-10-09T01:16:41Z
dc.creator.authorAlm-Kristiansen, Anne H
dc.creator.authorLorenzo, Petra I
dc.creator.authorMolværsmyr, Ann-Kristin
dc.creator.authorMatre, Vilborg
dc.creator.authorLedsaak, Marit
dc.creator.authorSæther, Thomas
dc.creator.authorGabrielsen, Odd S
dc.identifier.doihttp://dx.doi.org/10.1186/1476-4598-10-21
dc.identifier.urnURN:NBN:no-50645
dc.type.documentTidsskriftartikkel
dc.type.peerreviewedPeer reviewed
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/46459/1/12943_2010_Article_852.pdf
dc.type.versionPublishedVersion
cristin.articleid21


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