title: Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization.
abstract: The organization of the Golgi apparatus (GA) is tightly regulated. Golgi stack scattering is observed in cellular processes such as apoptosis and mitosis, and has also been associated with disruption of cellular lipid metabolism and neurodegenerative diseases. Our studies show that depletion of the human N-α-acetyltransferase 30 (hNaa30) induces fragmentation of the Golgi stack in HeLa and CAL-62 cell lines. The GA associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) was previously shown to require N-terminal acetylation for membrane association and based on its N-terminal sequence, it is likely to be a substrate of hNaa30. ARFRP1 is involved in endosome-to-trans-Golgi network (TGN) traffic. We observed that ARFRP1 shifted from a predominantlycis-Golgi and TGN localization to localizing both Golgi and non-Golgi vesicular structures in hNaa30-depleted cells. However, we did not observe loss of membrane association of ARFRP1. We conclude that hNaa30 depletion induces Golgi scattering and induces aberrant ARFRP1 Golgi localization.
authors.affiliation: Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.|Department of Molecular Medicine and Cancer Research, Center of Molecular Inflammation Research, Norwegian University of Technology and Natural Sciences, N-7006 Trondheim, Norway.
authors.forename: Kristian K
authors.initials: KK
authors.lastname: Starheim
authors.affiliation: Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
authors.forename: Thomas V
authors.initials: TV
authors.lastname: Kalvik
authors.affiliation: Department of Molecular Medicine and Cancer Research, Center of Molecular Inflammation Research, Norwegian University of Technology and Natural Sciences, N-7006 Trondheim, Norway.
authors.forename: Geir
authors.initials: G
authors.lastname: Bjørkøy
authors.affiliation: Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway thomas.arnesen@uib.no.|Department of Surgery, Haukeland University Hospital, N-5021 Bergen, Norway.
authors.forename: Thomas
authors.initials: T
authors.lastname: Arnesen
mesh_terms: D020727:ADP-Ribosylation Factors / Q000032:analysis / Q000378:metabolism*; D011992:Endosomes / Q000378:metabolism; D055785:Gene Knockdown Techniques; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D006367:HeLa Cells; D006801:Humans; D063211:N-Terminal Acetyltransferase C / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport; D021601:trans-Golgi Network / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D063211:N-Terminal Acetyltransferase C; C570950:NAA30 protein, human; D020727:ADP-Ribosylation Factors; C541296:ARFRP1 protein, human
keywords: ARFRP1; Golgi apparatus; N-terminal acetylation; NAT; Naa30; NatC