Evidence map›Paper›PMID 9480882›Full record

ArticleThe Biochemical journal1998

Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo.

M C Bañó, C S Jackson, A I Magee

Abstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Post-translational modification and regulation of actin.Current opinion in cell biology · 2013
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Article
  11. Palmitylation of cone opsins.Vision research · 2006
    Article
  12. Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Autopalmitoylation of tubulin.Protein science : a publication of the Protein Society · 2000
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

M C BañóDivision of Membrane Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW71AA, U.K.
C S Jackson
A I Magee

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Covalent attachment of a variety of lipid groups to proteins is now recognized as a major group of post-translational modifications. S-acylation of proteins at cysteine residues is the only modification considered dynamic and thus has the potential for regulating protein function and/or localization. The activities that catalyse reversible S-acylation have not been well characterized and it is not clear whether both the acylation and the deacylation steps are regulated, since in principle it would be sufficient to control only one of them. Both apparently enzymatic and non-enzymatic S-acylation of proteins have previously been reported. Here we show that a synthetic myristoylated c-Yes protein tyrosine kinase undecapeptide undergoes spontaneous S-acylation in vitro when using a long chain acyl-CoA as acyl donor in the absence of any protein. The S-acylation was dependent on myristoylation of the substrate, the length of the incubation period, temperature and substrate concentration. When COS cell fractions were added to the S-acylation reaction no additional peptide:S-acyltransferase activity was detected. These results are consistent with the possibility that membrane-associated proteins may undergo S-acylation in vivo by non-enzymatic transfer of acyl groups from acyl-CoA. In this case, the S-acylation-deacylation process could be controlled by a regulated depalmitoylation mechanism.

Indexed as

src-Family KinasesAcylationAnimalsCOS CellsElectrophoresis, Polyacrylamide GelHydrogen-Ion ConcentrationIntracellular MembranesMicrosomesModels, ChemicalMyristic AcidProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-yesMyristic AcidProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-yessrc-Family Kinases

Identifiers

PMID9480882
PMCPMC1219197

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.