PXD000930 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Naa30 is critically involved in maintaining mitochondrial and Golgi integrity |
Description | N-terminal acetylation is one of the most common protein modifications in eukaryotes, with emerging roles in regulating protein quality and stoichiometry and targeting and complex formation. The NatC complex is one of the three major N-terminal acetyltransferases (NATs). Here, we partially defined the in vivo human NatC Nt-acetylome by combining siNAA30 mediated knockdown with positional proteomics. We identified 51 human NatC substrates and expanded our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Tyr, Met-Trp, Met-Met, Met-His and Met-Lys N-termini. Next to cytosolic proteins, several organellar proteins were identified as NatC substrates. Interestingly, upon Naa30 depletion, the levels of several organellar proteins were reduced, in particular those of mitochondrial proteins. Further, knockdown of Naa30 induced the loss of membrane potential, clearing and fragmentation of mitochondria. Naa30 depletion also led to disassembly of the Golgi apparatus. However, Naa30 depletion did not affect ER morphology, endosome or peroxisome distribution or microtubule and actin cytoskeletal architecture, suggesting that the observed mitochondrial fragmentation and clearance and Golgi scattering are not due to general disruption of organelles or microtubules. In conclusion, NatC Nt-acetylates a large variety of cytosolic and organellar proteins and is essential for cis-Golgi integrity and mitochondrial function. |
HostingRepository | PRIDE |
AnnounceDate | 2016-10-05 |
AnnouncementXML | Submission_2016-10-05_05:20:43.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD000930 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Jonathan Vandenbussche |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | 6x(13)C: 4x(15)N labeled L-arginine; S-carboxymethyl-L-cysteine: 58.005479; 2-pyrrolidone-5-carboxylic acid (Gln): -17.026549; N-acetylated residue: 42.010565; 3x(2)H labeled N6-acetyl-L-lysine: 45.029395; L-methionine (S)-sulfoxide: 15.994915 |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2014-04-25 01:14:05 | ID requested | |
⏵ 1 | 2016-10-05 05:20:44 | announced | |
Publication List
Van Damme P, Kalvik TV, Starheim KK, Jonckheere V, Myklebust LM, Menschaert G, Varhaug JE, Gevaert K, Arnesen T, A Role for Human N-alpha Acetyltransferase 30 (Naa30) in Maintaining Mitochondrial Integrity. Mol Cell Proteomics, 15(11):3361-3372(2016) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: human, Naa30, Golgi, Mitochondria, N-terminal COFRADIC |
Contact List
Kris Gevaert |
contact affiliation | University Ghent, VIB |
contact email | kris.gevaert@ugent.be |
lab head | |
Jonathan Vandenbussche |
contact affiliation | Biochemistry |
contact email | jonathan.vandenbussche@vib-ugent.be |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD000930
- Label: PRIDE project
- Name: Naa30 is critically involved in maintaining mitochondrial and Golgi integrity