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dc.contributor.authorAksnes, Henrietteen_US
dc.contributor.authorVan Damme, Petraen_US
dc.contributor.authorGoris, Marianneen_US
dc.contributor.authorStarheim, Kristian K.en_US
dc.contributor.authorMarie, Michael Bruno Ericen_US
dc.contributor.authorStøve, Svein Isungseten_US
dc.contributor.authorHoel, Camillaen_US
dc.contributor.authorKalvik, Thomas Vikestaden_US
dc.contributor.authorHole, Kristineen_US
dc.contributor.authorGlomnes, Ninaen_US
dc.contributor.authorFurnes, Clemensen_US
dc.contributor.authorLjostveit, Sonjaen_US
dc.contributor.authorZiegler, Mathiasen_US
dc.contributor.authorNiere, Marcen_US
dc.contributor.authorGevaert, Krisen_US
dc.contributor.authorArnesen, Thomasen_US
dc.PublishedCell reports 2015, 10(8):1362-1374eng
dc.description.abstractN-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or Nα-acetyltransferase 60 (Naa60), was recently identified as a NAT in multicellular eukaryotes. Here, we find that Naa60 differs from all other known NATs by its Golgi localization. A new membrane topology assay named PROMPT and a selective membrane permeabilization assay established that Naa60 faces the cytosolic side of intracellular membranes. An Nt-acetylome analysis of NAA60-knockdown cells revealed that Naa60, as opposed to other NATs, specifically acetylates transmembrane proteins and has a preference for N termini facing the cytosol. Moreover, NAA60 knockdown causes Golgi fragmentation, indicating an important role in the maintenance of the Golgi’s structural integrity. This work identifies a NAT associated with membranous compartments and establishes N-terminal acetylation as a common modification among transmembrane proteins, a thus-far poorly characterized part of the N-terminal acetylome.en_US
dc.rightsAttribution CC BY-NC-ND 3.0eng
dc.titleAn organellar Nα-acetyltransferase, Naa60, acetylates cytosolic n termini of transmembrane proteins and maintains golgi integrityen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2015 The Authors
dc.subject.nsiVDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk molekylærbiologi : 711
dc.subject.nsiVDP::Midical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical molecular biology: 711
dc.subject.nsiVDP::Matematikk og Naturvitenskap: 400en_US

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Attribution CC BY-NC-ND 3.0
Except where otherwise noted, this item's license is described as Attribution CC BY-NC-ND 3.0