Evidence map›Paper›PMID 24411241›Full record

ArticleBiophysical journal2014

The autodepalmitoylating activity of APT maintains the spatial organization of palmitoylated membrane proteins.

Nachiket Vartak, Bjoern Papke, Hernan E Grecco, Lisaweta Rossmannek, Herbert Waldmann, Christian Hedberg, Philippe I H Bastiaens

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

58 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Biochemistry · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  13. Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.American journal of physiology. Cell physiology · 2024
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. Pathogens (Basel, Switzerland) · 2022
    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

7 authors at 2 institutions in 1 country.

Nachiket VartakDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany.
Bjoern PapkeDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany.
Hernan E GreccoDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany.
Lisaweta RossmannekDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany.
Herbert WaldmannDepartment of Chemical Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany; Faculty of Chemistry, Technical University Dortmund, Dortmund, Germany.
Christian HedbergDepartment of Chemical Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany.
Philippe I H BastiaensDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, Dortmund, Germany; Faculty of Chemistry, Technical University Dortmund, Dortmund, Germany. Electronic address: philippe.bastiaens@mpi-dortmund.mpg.de.
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The localization and signaling of S-palmitoylated peripheral membrane proteins is sustained by an acylation cycle in which acyl protein thioesterases (APTs) depalmitoylate mislocalized palmitoylated proteins on endomembranes. However, the APTs are themselves reversibly S-palmitoylated, which localizes thioesterase activity to the site of the antagonistc palmitoylation activity on the Golgi. Here, we resolve this conundrum by showing that palmitoylation of APTs is labile due to autodepalmitoylation, creating two interconverting thioesterase pools: palmitoylated APT on the Golgi and depalmitoylated APT in the cytoplasm, with distinct functionality. By imaging APT-substrate catalytic intermediates, we show that it is the depalmitoylated soluble APT pool that depalmitoylates substrates on all membranes in the cell, thereby establishing its function as release factor of mislocalized palmitoylated proteins in the acylation cycle. The autodepalmitoylating activity on the Golgi constitutes a homeostatic regulation mechanism of APT levels at the Golgi that ensures robust partitioning of APT substrates between the plasma membrane and the Golgi.

Indexed as

Protein Processing, Post-TranslationalAcylationAnimalsCytoplasmDogsGolgi ApparatusLipoylationMadin Darby Canine Kidney CellsProtein TransportThiolester HydrolasesThiolester Hydrolases

Identifiers

PMID24411241
PMCPMC3907232
OpenAlexW2068612489

What OpenQuestion holds

Textmetadata
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.