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dc.contributor.authorAksnes, Henriette
dc.contributor.authorDrazic, Adrian
dc.contributor.authorMarie, Michael Bruno Eric
dc.contributor.authorArnesen, Thomas
dc.date.accessioned2017-06-01T08:31:06Z
dc.date.available2017-06-01T08:31:06Z
dc.date.issued2016-09
dc.PublishedAksnes H, Drazic A, Marie MBE, Arnesen TA. First Things First: Vital Protein Marks by N-Terminal Acetyltransferases. TIBS -Trends in Biochemical Sciences. Regular ed. 2016;41(9):746-760eng
dc.identifier.issn0968-0004en_US
dc.identifier.urihttps://hdl.handle.net/1956/15909
dc.description.abstractN-terminal (Nt) acetylation is known to be a highly abundant co-translational protein modification, but the recent discovery of Golgi- and chloroplast-resident N-terminal acetyltransferases (NATs) revealed that it can also be added post-translationally. Nt-acetylation may act as a degradation signal in a novel branch of the N-end rule pathway, whose functions include the regulation of human blood pressure. Nt-acetylation also modulates protein interactions, targeting, and folding. In plants, Nt-acetylation plays a role in the control of resistance to drought and in regulation of immune responses. Mutations of specific human NATs that decrease their activity can cause either the lethal Ogden syndrome or severe intellectual disability and cardiovascular defects. In sum, recent advances highlight Nt-acetylation as a key factor in many biological pathways.en_US
dc.language.isoengeng
dc.publisherElsevieren_US
dc.relation.urihttp://www.sciencedirect.com/science/article/pii/S0968000416300779
dc.rightsAttribution CC BY-NC-NDeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/eng
dc.subjectN-terminal acetyltransferase (NAT)eng
dc.subjectNα-acetyltransferase (Naa)eng
dc.subjectN-terminal acetylationeng
dc.subjectprotein interactionseng
dc.subjectprotein foldingeng
dc.subjectprotein stabilityeng
dc.titleFirst Things First: Vital Protein Marks by N-Terminal Acetyltransferasesen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2017-05-09T09:54:04Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2016 The Author(s)en_US
dc.identifier.doihttps://doi.org/10.1016/j.tibs.2016.07.005
dc.identifier.cristin1448261
dc.source.journalTIBS -Trends in Biochemical Sciences. Regular ed.


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