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An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity

Henriette Aksnes, Petra Van Damme UGent, Marianne Goris, Kristian K Starheim, Michaël Marie, Svein Isungset Støve, Camilla Hoel, Thomas Vikestad Kalvik, Kristine Hole, Nina Glomnes, et al. (2015) CELL REPORTS. 10(8). p.1362-1374
abstract
N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or N alpha-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.
Please use this url to cite or link to this publication:
author
organization
alternative title
An organellar N alpha-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity
year
type
journalArticle (original)
publication status
published
subject
keyword
DROSOPHILA, INSIGHTS, ORGANIZATION, CONSERVATION, MICROTUBULES, YEAST, COMPLEX, GTPASE ARL3P, MEMBRANE-PROTEIN, SACCHAROMYCES-CEREVISIAE
journal title
CELL REPORTS
Cell Reports
volume
10
issue
8
pages
1362 - 1374
Web of Science type
Article
Web of Science id
000350564200013
JCR category
CELL BIOLOGY
JCR impact factor
7.87 (2015)
JCR rank
26/187 (2015)
JCR quartile
1 (2015)
ISSN
2211-1247
DOI
10.1016/j.celrep.2015.01.053
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
5928546
handle
http://hdl.handle.net/1854/LU-5928546
date created
2015-04-08 11:20:12
date last changed
2017-07-24 13:58:10
@article{5928546,
  abstract     = {N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or N alpha-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.},
  author       = {Aksnes, Henriette and Van Damme, Petra and Goris, Marianne and Starheim, Kristian K and Marie, Micha{\"e}l and St{\o}ve, Svein Isungset and Hoel, Camilla and Kalvik, Thomas Vikestad and Hole, Kristine and Glomnes, Nina and Furnes, Clemens and Ljostveit, Sonja and Ziegler, Mathias and Niere, Marc and Gevaert, Kris and Arnesen, Thomas},
  issn         = {2211-1247},
  journal      = {CELL REPORTS},
  keyword      = {DROSOPHILA,INSIGHTS,ORGANIZATION,CONSERVATION,MICROTUBULES,YEAST,COMPLEX,GTPASE ARL3P,MEMBRANE-PROTEIN,SACCHAROMYCES-CEREVISIAE},
  language     = {eng},
  number       = {8},
  pages        = {1362--1374},
  title        = {An organellar N\ensuremath{\alpha}-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity},
  url          = {http://dx.doi.org/10.1016/j.celrep.2015.01.053},
  volume       = {10},
  year         = {2015},
}

Chicago
Aksnes, Henriette, Petra Van Damme, Marianne Goris, Kristian K Starheim, Michaël Marie, Svein Isungset Støve, Camilla Hoel, et al. 2015. “An Organellar Nα-acetyltransferase, Naa60, Acetylates Cytosolic N Termini of Transmembrane Proteins and Maintains Golgi Integrity.” Cell Reports 10 (8): 1362–1374.
APA
Aksnes, H., Van Damme, P., Goris, M., Starheim, K. K., Marie, M., Støve, S. I., Hoel, C., et al. (2015). An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. CELL REPORTS, 10(8), 1362–1374.
Vancouver
1.
Aksnes H, Van Damme P, Goris M, Starheim KK, Marie M, Støve SI, et al. An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. CELL REPORTS. 2015;10(8):1362–74.
MLA
Aksnes, Henriette, Petra Van Damme, Marianne Goris, et al. “An Organellar Nα-acetyltransferase, Naa60, Acetylates Cytosolic N Termini of Transmembrane Proteins and Maintains Golgi Integrity.” CELL REPORTS 10.8 (2015): 1362–1374. Print.