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dc.contributor.authorStabell, Marianne
dc.contributor.authorSæther, Thomas
dc.contributor.authorKjendseth, Åsmund Røhr
dc.contributor.authorGabrielsen, Odd Stokke
dc.contributor.authorMyklebost, Ola
dc.date.accessioned2021-03-23T09:45:32Z
dc.date.available2021-03-23T09:45:32Z
dc.date.created2021-03-19T09:05:53Z
dc.date.issued2021
dc.identifier.citationBiochemical and Biophysical Research Communications - BBRC. 2021, 552, 91-97.en_US
dc.identifier.issn0006-291X
dc.identifier.urihttps://hdl.handle.net/11250/2735002
dc.description.abstractHigh mobility group A2 (HMGA2) is a chromatin-associated protein involved in the regulation of stem cell function, embryogenesis and cancer development. Although the protein does not contain a consensus SUMOylation site, it is shown to be SUMOylated. In this study, we demonstrate that the first lysine residue in the reported K66KAE SUMOylation motif in HMGA2 can be methylated in vitro and in vivo by the Set7/9 methyltransferase. By editing the lysine, the increased hydrophobicity of the resulting 6-N-methyl-lysine transforms the sequence into a consensus SUMO motif. This post-translational editing dramatically increases the subsequent SUMOylation of this site. Furthermore, similar putative methylation-dependent SUMO motifs are found in a number of other chromatin factors, and we confirm methylation-dependent SUMOylation of a site in one such protein, the Polyhomeotic complex 1 homolog (PHC1). Together, these results suggest that crosstalk between methylation and SUMOylation is a general mode for regulation of chromatin function.en_US
dc.language.isoengen_US
dc.relation.urihttps://doi.org/10.1016/j.bbrc.2021.02.099
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/deed.no*
dc.titleMethylation-dependent SUMOylation of the architectural transcription factor HMGA2en_US
dc.typePeer revieweden_US
dc.typeJournal articleen_US
dc.description.versionpublishedVersionen_US
dc.source.pagenumber91-97en_US
dc.source.volume552en_US
dc.source.journalBiochemical and Biophysical Research Communications - BBRCen_US
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2021.02.099
dc.identifier.cristin1899186
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal
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