Evidence map›Paper›PMID 20334580›Full record

ArticleMolecular membrane biology2010

DHHC20: a human palmitoyl acyltransferase that causes cellular transformation.

Jeremiah M Draper, Charles D Smith

Open access · bronzeAbstract read
In one paragraph

Article in Molecular membrane biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  5. Review
  6. The Mechanism of Selective Recognition of Lipid Substrate by hDHHC20 Enzyme.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Palmitoylation: a proteinNPJ breast cancer · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Lipid biology of breast cancer.Biochimica et biophysica acta · 2013
    Review
  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.

Jeremiah M DraperDepartment of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA.
Charles D Smith
Medical University of South Carolina · US

Funding

ACYLTRANSFERASE INHIBITORS AS ANTI RAS AGENTSR01CA075248 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI SMITH, CHARLES D. · 1997 to 2009
$2.2M
NCI NIH HHS 2 R01 CA075248NCI NIH HHS R01 CA075248
6 · The paper itself

Abstract

Palmitoylation is required for the activities of several cancer-associated proteins, making the palmitoyl acyltransferase (PAT) enzymes that catalyze these reactions potential targets for anticancer therapeutics. In this study, we sought to identify and characterize a human PAT with activity toward N-terminally myristoylated and palmitoylated proteins. NIH/3t3 cells were stably transfected with vectors containing no insert, wild type human DHHC20, or a serine-substituted DHHS20 mutant. Compared with control cells, cells overexpressing wild-type DHHC20 displayed an increase in palmitoylation activity toward a peptide that mimics the N-terminus of myristoylated and palmitoylated proteins, but had no change in activity toward a peptide that mimics the C-terminus of farnesylated and palmitoylated proteins. Cells expressing DHHS20 had no significant change in activity toward either peptide. Overexpression of DHHC20 also caused phenotypic changes consistent with cellular transformation, including colony formation in soft agar, decreased contact inhibition of growth, and increased proliferation under low-serum conditions. Quantitative polymerase chain reaction analyses of human tissues demonstrated that DHHC20 is expressed in a tissue-specific manner, and is overexpressed in several types of human tumors, including ovarian, breast and prostate. Overall, these results demonstrate that DHHC20 is a human N-terminal-myristoyl-directed PAT involved in cellular transformation, that may play a role in cancer.

Indexed as

AcyltransferasesAnimalsCell Line, TumorCell ProliferationCell Transformation, NeoplasticGene Expression ProfilingGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansLipoylationMiceNIH 3T3 CellsRNA, MessengerTransfectionAcyltransferasesRNA, MessengerZDHHC20 protein, human

Identifiers

PMID20334580
PMCPMC2893407
OpenAlexW2033802894

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.