dc.contributor.author | Aksnes, Henriette | en_US |
dc.contributor.author | Van Damme, Petra | en_US |
dc.contributor.author | Goris, Marianne | en_US |
dc.contributor.author | Starheim, Kristian K. | en_US |
dc.contributor.author | Marie, Michael Bruno Eric | en_US |
dc.contributor.author | Støve, Svein Isungset | en_US |
dc.contributor.author | Hoel, Camilla | en_US |
dc.contributor.author | Kalvik, Thomas Vikestad | en_US |
dc.contributor.author | Hole, Kristine | en_US |
dc.contributor.author | Glomnes, Nina | en_US |
dc.contributor.author | Furnes, Clemens | en_US |
dc.contributor.author | Ljostveit, Sonja | en_US |
dc.contributor.author | Ziegler, Mathias | en_US |
dc.contributor.author | Niere, Marc | en_US |
dc.contributor.author | Gevaert, Kris | en_US |
dc.contributor.author | Arnesen, Thomas | en_US |
dc.date.accessioned | 2016-01-14T10:29:11Z | |
dc.date.available | 2016-01-14T10:29:11Z | |
dc.date.issued | 2015-02-26 | |
dc.Published | Cell reports 2015, 10(8):1362-1374 | eng |
dc.identifier.issn | 2211-1247 | |
dc.identifier.uri | https://hdl.handle.net/1956/10959 | |
dc.description.abstract | N-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.language.iso | eng | eng |
dc.publisher | Elsevier | eng |
dc.rights | Attribution CC BY-NC-ND 3.0 | eng |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0 | eng |
dc.subject | Naa60 | eng |
dc.subject | PROMPT | eng |
dc.title | An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic n termini of transmembrane proteins and maintains golgi integrity | en_US |
dc.type | Peer reviewed | |
dc.type | Journal article | |
dc.date.updated | 2015-12-21T20:07:52Z | |
dc.description.version | publishedVersion | en_US |
dc.rights.holder | Copyright 2015 The Authors | |
dc.identifier.doi | https://doi.org/10.1016/j.celrep.2015.01.053 | |
dc.identifier.cristin | 1239253 | |
dc.subject.nsi | VDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk molekylærbiologi : 711 | |
dc.subject.nsi | VDP::Midical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical molecular biology: 711 | |
dc.subject.nsi | VDP::Matematikk og Naturvitenskap: 400 | en_US |