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A role for human N-alpha acetyltransferase 30 (Naa30) in maintaining mitochondrial integrity

Petra Van Damme UGent, Thomas V Kalvik, Kristian W Starheim, Veronique Jonckheere UGent, Line M Myklebust, Gerben Menschaert UGent, Jan Erik Varhaug, Kris Gevaert UGent and Thomas Arnesen (2016) MOLECULAR & CELLULAR PROTEOMICS. 15(11). p.3361-3372
abstract
N-terminal acetylation (Nt-acetylation) by N-terminal acetyltransferases (NATs) is one of the most common protein modifications in eukaryotes. The NatC complex represents one of three major NATs of which the substrate profile remains largely unexplored. Here, we defined the in vivo human NatC Nt-acetylome on a proteome-wide scale by combining knockdown of its catalytic subunit Naa30 with positional proteomics. We identified 46 human NatC substrates, expanding our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Val, Met-Met, Met-His and Met-Lys N termini. Upon Naa30 depletion the expression levels of several organellar proteins were found reduced, in particular mitochondrial proteins, some of which were found to be NatC substrates. Interestingly, knockdown of Naa30 induced the loss of mitochondrial membrane potential and fragmentation of mitochondria. In conclusion, NatC N-tacetylates a large variety of proteins and is essential for mitochondrial integrity and function.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
MEMBRANE-PROTEIN SYS1P, ARF-LIKE GTPASE, TERMINAL ACETYLATION, SACCHAROMYCES-CEREVISIAE, YEAST, DEGRADATION, PROTEOMICS, MITOPHAGY, APOPTOSIS, COMPLEX
journal title
MOLECULAR & CELLULAR PROTEOMICS
Mol. Cell. Proteomics
volume
15
issue
11
pages
3361 - 3372
Web of Science type
Article
Web of Science id
000387505500003
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
6.54 (2016)
JCR rank
5/77 (2016)
JCR quartile
1 (2016)
ISSN
1535-9476
DOI
10.1074/mcp.M116.061010
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
8198267
handle
http://hdl.handle.net/1854/LU-8198267
date created
2016-11-29 17:47:53
date last changed
2017-07-13 09:32:30
@article{8198267,
  abstract     = {N-terminal acetylation (Nt-acetylation) by N-terminal acetyltransferases (NATs) is one of the most common protein modifications in eukaryotes. The NatC complex represents one of three major NATs of which the substrate profile remains largely unexplored. Here, we defined the in vivo human NatC Nt-acetylome on a proteome-wide scale by combining knockdown of its catalytic subunit Naa30 with positional proteomics. We identified 46 human NatC substrates, expanding our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Val, Met-Met, Met-His and Met-Lys N termini. Upon Naa30 depletion the expression levels of several organellar proteins were found reduced, in particular mitochondrial proteins, some of which were found to be NatC substrates. Interestingly, knockdown of Naa30 induced the loss of mitochondrial membrane potential and fragmentation of mitochondria. In conclusion, NatC N-tacetylates a large variety of proteins and is essential for mitochondrial integrity and function.},
  author       = {Van Damme, Petra and Kalvik, Thomas V and Starheim, Kristian W and Jonckheere, Veronique and Myklebust, Line M and Menschaert, Gerben and Varhaug, Jan Erik and Gevaert, Kris and Arnesen, Thomas},
  issn         = {1535-9476},
  journal      = {MOLECULAR \& CELLULAR PROTEOMICS},
  keyword      = {MEMBRANE-PROTEIN SYS1P,ARF-LIKE GTPASE,TERMINAL ACETYLATION,SACCHAROMYCES-CEREVISIAE,YEAST,DEGRADATION,PROTEOMICS,MITOPHAGY,APOPTOSIS,COMPLEX},
  language     = {eng},
  number       = {11},
  pages        = {3361--3372},
  title        = {A role for human N-alpha acetyltransferase 30 (Naa30) in maintaining mitochondrial integrity},
  url          = {http://dx.doi.org/10.1074/mcp.M116.061010},
  volume       = {15},
  year         = {2016},
}

Chicago
Van Damme, Petra, Thomas V Kalvik, Kristian W Starheim, Veronique Jonckheere, Line M Myklebust, Gerben Menschaert, Jan Erik Varhaug, Kris Gevaert, and Thomas Arnesen. 2016. “A Role for Human N-alpha Acetyltransferase 30 (Naa30) in Maintaining Mitochondrial Integrity.” Molecular & Cellular Proteomics 15 (11): 3361–3372.
APA
Van Damme, Petra, Kalvik, T. V., Starheim, K. W., Jonckheere, V., Myklebust, L. M., Menschaert, G., Varhaug, J. E., et al. (2016). A role for human N-alpha acetyltransferase 30 (Naa30) in maintaining mitochondrial integrity. MOLECULAR & CELLULAR PROTEOMICS, 15(11), 3361–3372.
Vancouver
1.
Van Damme P, Kalvik TV, Starheim KW, Jonckheere V, Myklebust LM, Menschaert G, et al. A role for human N-alpha acetyltransferase 30 (Naa30) in maintaining mitochondrial integrity. MOLECULAR & CELLULAR PROTEOMICS. 2016;15(11):3361–72.
MLA
Van Damme, Petra, Thomas V Kalvik, Kristian W Starheim, et al. “A Role for Human N-alpha Acetyltransferase 30 (Naa30) in Maintaining Mitochondrial Integrity.” MOLECULAR & CELLULAR PROTEOMICS 15.11 (2016): 3361–3372. Print.