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http://purl.uniprot.org/citations/25732826http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25732826http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25732826http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/25732826http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.01.053"xsd:string
http://purl.uniprot.org/citations/25732826http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.01.053"xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Arnesen T."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Arnesen T."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Gevaert K."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Gevaert K."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Hole K."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Hole K."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Kalvik T.V."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Kalvik T.V."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Van Damme P."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Van Damme P."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Stoeve S.I."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Stoeve S.I."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Aksnes H."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Aksnes H."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Glomnes N."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Glomnes N."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Marie M."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Marie M."xsd:string
http://purl.uniprot.org/citations/25732826http://purl.uniprot.org/core/author"Niere M."xsd:string