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@ARTICLE{Nuskova:277800,
      author       = {H. Nuskova$^*$ and F. G. Cortizo$^*$ and L. S.
                      Schwenker$^*$ and T. Sachsenheimer and E. Diakonov$^*$ and
                      M. Tiebe$^*$ and M. Schneider$^*$ and J. Lohbeck$^*$ and C.
                      Reid$^*$ and A. Kopp-Schneider$^*$ and D. Helm$^*$ and B.
                      Brügger and A. K. Miller$^*$ and A. Teleman$^*$},
      title        = {{C}ompetition for cysteine acylation by {C}16:0 and {C}18:0
                      derived lipids is a global phenomenon in the proteome.},
      journal      = {The journal of biological chemistry},
      volume       = {299},
      number       = {9},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2023-01511},
      pages        = {105088},
      year         = {2023},
      note         = {#EA:B140#LA:B140# / 2023 Jul 24;299(9):105088},
      abstract     = {S-acylation is a reversible posttranslational protein
                      modification consisting of attachment of a fatty acid to a
                      cysteine via a thioester bond. Research over the last few
                      years has shown that a variety of different fatty acids,
                      such as palmitic acid (C16:0), stearate (C18:0) or oleate
                      (C18:1), are used in cells to S-acylate proteins. We
                      recently showed that GNAI proteins can be acylated on a
                      single residue, Cys3, with either C16:0 or C18:1 and that
                      the relative proportion of acylation with these fatty acids
                      depends on the level of the respective fatty acid in the
                      cell's environment. This has functional consequences for
                      GNAI proteins, with the identity of the acylating fatty acid
                      affecting the subcellular localization of GNAIs. Unclear is
                      whether this competitive acylation is specific to GNAI
                      proteins or a more general phenomenon in the proteome. We
                      perform here a proteome screen to identify proteins acylated
                      with different fatty acids. We identify 218 proteins
                      acylated with C16:0 and 308 proteins acylated with
                      C18-lipids, thereby uncovering novel targets of acylation.
                      We find that most proteins that can be acylated by C16:0 can
                      also be acylated with C18-fatty acids. For proteins with
                      more than one acylation site, we find that this competitive
                      acylation occurs on each individual cysteine residue. This
                      raises the possibility that the function of many different
                      proteins can be regulated by the lipid environment via
                      differential S-acylation.},
      keywords     = {HRAS (Other) / LAMTOR1 (Other) / S-oleoylation (Other) /
                      S-palmitoylation (Other) / S-stearoylation (Other) / click
                      chemistry (Other) / lipid (Other) / posttranslational
                      modification (Other) / protein S-acylation (Other) /
                      transferrin receptor 1 (Other)},
      cin          = {B140 / W120 / A390 / C060},
      ddc          = {540},
      cid          = {I:(DE-He78)B140-20160331 / I:(DE-He78)W120-20160331 /
                      I:(DE-He78)A390-20160331 / I:(DE-He78)C060-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37495107},
      doi          = {10.1016/j.jbc.2023.105088},
      url          = {https://inrepo02.dkfz.de/record/277800},
}