Evidence map›Paper›PMID 19416974›Full record

ArticleThe Journal of biological chemistry2009

Molecular recognition of the palmitoylation substrate Vac8 by its palmitoyltransferase Pfa3.

Marissa J Nadolski, Maurine E Linder

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  3. Review
  4. The Journal of biological chemistry · 2020
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. The physiology of protein S-acylation.Physiological reviews · 2015
    Review
  14. Substrate recognition by the cell surface palmitoyl transferase DHHC5.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. Article
  18. Palmitoylation of virus proteins.Biology of the cell · 2012
    Review
  19. 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

2 authors at 1 institution in 1 country.

Marissa J NadolskiDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Maurine E Linder
Washington University in St. Louis · US

Funding

TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGYT32GM007067 · NIGMS · WASHINGTON UNIVERSITY · PI TRUE-KROB, HEATHER L · 1985 to 2020
$20.4M
PROTEIN PALMITOYLATION IN SIGNALING SYSTEMSR01GM051466 · NIGMS · WASHINGTON UNIVERSITY · PI LINDER, MAURINE E · 1994 to 2010
$3.2M
NIGMS NIH HHS GM51466NIGMS NIH HHS R01 GM051466NIGMS NIH HHS T32GM07067
6 · The paper itself

Abstract

Palmitoylation of the yeast vacuolar protein Vac8 is important for its role in membrane-mediated events such as vacuole fusion. It has been established both in vivo and in vitro that Vac8 is palmitoylated by the Asp-His-His-Cys (DHHC) protein Pfa3. However, the determinants of Vac8 critical for recognition by Pfa3 have yet to be elucidated. This is of particular importance because of the lack of a consensus sequence for palmitoylation. Here we show that Pfa3 was capable of palmitoylating each of the three N-terminal cysteines of Vac8 and that this reaction was most efficient when Vac8 is N-myristoylated. Additionally, when we analyzed the Src homology 4 (SH4) domain of Vac8 independent of the rest of the protein, palmitoylation by Pfa3 still occurred. However, the specificity of palmitoylation seen for the full-length protein was lost, and the SH4 domain was palmitoylated by all five of the yeast DHHC proteins tested. These data suggested that a region of the protein C-terminal to the SH4 domain was important for conferring specificity of palmitoylation. This was confirmed by use of a chimeric protein in which the SH4 domain of Vac8 was swapped for that of Meh1, another palmitoylated and N-myristoylated protein in yeast. In this case we saw specificity mimic that of wild type Vac8. Competition experiments revealed that the 11th armadillo repeat of Vac8 is an important element for recognition by Pfa3. This demonstrates that regions distant from the palmitoylated cysteines are important for recognition by DHHC proteins.

Indexed as

AcetyltransferasesAcyltransferasesAmino Acid SequenceAspartic AcidCysteineHistidineLipoylationMolecular Sequence DataMutagenesis, Site-DirectedRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino Acidsrc Homology DomainsVacuolesVesicular Transport ProteinsAcetyltransferasesAcyltransferasesAspartic AcidCysteineHistidinePfa3 protein, S cerevisiaeprotein acyltransferaseRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVAC8 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID19416974
PMCPMC2719411
OpenAlexW2077141717

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.