<< Full experiment listing

PXD006856

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2018-10-24
  • AnnouncementXML: Submission_2018-10-24_11:35:55.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Evy Timmerman
  • Title: Naa80 acetylates the actin N-terminus impacting the actin cytoskeleton and cell motility
  • Description: Eukaryotic actins undergo several post-translational modifications during their maturation to enable a fully functional cytoskeletal network. A unique N-terminal processing is conserved in the animal kingdom and includes the removal of the first one or two amino acids as well as N-terminal acetylation of the newly exposed acidic N-termini. These events have been known for decades, but the mechanism and function of actin N-terminal acetylation are not well understood due to the lack of information on the catalysing N-terminal acetyltransferase (NAT). Here, we show that NAA80, previously known as NAT6 or FUS-2,is a unique, animal kingdom-specific NAT that exclusively N-terminally acetylates actins. In vitro, the lack of actin N-terminal acetylation impedes the actin polymerization rate due to decreased formin-mediated filament elongation, while the depolymerisation rate is unaffected. Human NAA80 knockout cells display a complete loss of actin N-terminal acetylation and a reorganization of the actin cytoskeleton. We reveal Naa80 as the enzyme that specifically N-terminally acetylates actin the most abundant protein in animal cells, and that this modification controls cellular dynamics and cytoskeletal functions. In this project acetylation of actins was investigated with the use of LC-MS/MS and MS1 quantitation of the Total Ion Current signal.
  • SpeciesList: scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
  • ModificationList: monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
  • Instrument: Q Exactive HF

Dataset History

VersionDatetimeStatusChangeLog Entry
02017-07-03 03:35:30ID requested
12018-10-24 11:35:56announced

Publication List

  1. Drazic A, Aksnes H, Marie M, Boczkowska M, Varland S, Timmerman E, Foyn H, Glomnes N, Rebowski G, Impens F, Gevaert K, Dominguez R, Arnesen T, NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility. Proc Natl Acad Sci U S A, 115(17):4399-4404(2018) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: human, NAT, actin, N-terminal acetylation

Contact List

    Thomas Arnesen
    • contact affiliation: Department of Molecular Biology, University of Bergen, N-5020 Bergen
    • contact email: Thomas.Arnesen@uib.no
    • lab head:
    Evy Timmerman
    • contact affiliation: Ghent University - VIB
    • contact email: evy.timmerman@vib-ugent.be
    • dataset submitter:

Full Dataset Link List

  1. Dataset FTP location
  2. PRIDE project URI
Repository Record List
[+]

If you have a question or comment about ProteomeXchange, please contact us!
to receive all new ProteomeXchange dataset release announcements!