Evidence map›Paper›PMID 26701913›Full record

ArticleeLife2015

ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization.

David Tse Shen Lin, Elizabeth Conibear

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed, 2 pooled it
8.3field-weighted citation impact, top 1% 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

211 citing papers in PubMed, 2 syntheses or guidelines pooled it, 327 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. Article
  6. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Biochemistry · 2026
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

151 more citing papers are in PubMed but not listed here.

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.

David Tse Shen LinCentre for Molecular Medicine and Therapeutics, University of British Columbia, Vancouver, Canada.ORCID http://orcid.org/0000-0001-5695-9446
Elizabeth ConibearCentre for Molecular Medicine and Therapeutics, University of British Columbia, Vancouver, Canada.
University of British Columbia · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Dynamic changes in protein S-palmitoylation are critical for regulating protein localization and signaling. Only two enzymes - the acyl-protein thioesterases APT1 and APT2 - are known to catalyze palmitate removal from cytosolic cysteine residues. It is unclear if these enzymes act constitutively on all palmitoylated proteins, or if additional depalmitoylases exist. Using a dual pulse-chase strategy comparing palmitate and protein half-lives, we found knockdown or inhibition of APT1 and APT2 blocked depalmitoylation of Huntingtin, but did not affect palmitate turnover on postsynaptic density protein 95 (PSD95) or N-Ras. We used activity profiling to identify novel serine hydrolase targets of the APT1/2 inhibitor Palmostatin B, and discovered that a family of uncharacterized ABHD17 proteins can accelerate palmitate turnover on PSD95 and N-Ras. ABHD17 catalytic activity is required for N-Ras depalmitoylation and re-localization to internal cellular membranes. Our findings indicate that the family of depalmitoylation enzymes may be substantially broader than previously believed.

Indexed as

Gene Expression RegulationProtein Processing, Post-TranslationalAnimalsCell LineDisks Large Homolog 4 ProteinGTP PhosphohydrolasesHumansIntracellular MembranesIntracellular Signaling Peptides and ProteinsMembrane ProteinsPalmitatesProtein TransportDisks Large Homolog 4 ProteinDLG4 protein, humanGTP PhosphohydrolasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsNRAS protein, humanPalmitatesABHD17AABHD17BABHD17CAcyl Protein ThioesteraseAPT1biochemistrycell biologydepalmitoylationFAM108A1FAM108B1FAM108C1humanN-RaspalmitoylationPalmostatin BPSD95

Identifiers

PMID26701913
PMCPMC4755737
OpenAlexW2288301981

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.