Evidence map›Paper›PMID 20156967›Full record

ArticleThe Journal of cell biology2010

Unconventional secretion of Acb1 is mediated by autophagosomes.

Juan M Duran, Christophe Anjard, Chris Stefan, William F Loomis, Vivek Malhotra

Abstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
254citing papers in PubMed, 2 pooled it
15.1field-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

254 citing papers in PubMed, 2 syntheses or guidelines pooled it, 425 citations in OpenAlex.

  1. Guideline
  2. Guideline
  3. Article
  4. Article
  5. Review
  6. A Nanoparticle-Integrated Complete Manufacturing Pipeline of Chemically Engineered Exosomes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Endocytic tethers modulate unconventional GAPDH secretion.Cell surface (Amsterdam, Netherlands) · 2025
    Article
  14. Unconventional secretion of PARK7 requires lysosomal delivery via chaperone-mediated autophagy and specialized SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Juan M DuranCenter for Genomic Regulation, Barcelona 08003, Spain.
Christophe Anjard
Chris Stefan
William F Loomis
Vivek Malhotra
University of California, San Diego · USCentre for Genomic Regulation · ESCornell University · USInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

Intercellular signaling during terminal differentiationR01GM078175 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LOOMIS, WILLIAM F · 2006 to 2009
$1.0M
NIGMS NIH HHS GM78175NIGMS NIH HHS R01 GM078175
6 · The paper itself

Abstract

Starving Dictyostelium discoideum cells secrete AcbA, an acyl coenzyme A-binding protein (ACBP) that lacks a conventional signal sequence for entering the endoplasmic reticulum (ER). Secretion of AcbA in D. discoideum requires the Golgi-associated protein GRASP. In this study, we report that starvation-induced secretion of Acb1, the Saccharomyces cerevisiae ACBP orthologue, also requires GRASP (Grh1). This highlights the conserved function of GRASP in unconventional secretion. Although genes required for ER to Golgi or Golgi to cell surface transport are not required for Acb1 secretion in yeast, this process involves autophagy genes and the plasma membrane t-SNARE, Sso1. Inhibiting transport to vacuoles does not affect Acb1 secretion. In sum, our experiments reveal a unique secretory pathway where autophagosomes containing Acb1 evade fusion with the vacuole to prevent cargo degradation. We propose that these autophagosome intermediates fuse with recycling endosomes instead to form multivesicular body carriers that then fuse with the plasma membrane to release cargo.

Indexed as

AutophagyAmino Acid SequenceCarrier ProteinsCell MembraneGenes, FungalGolgi ApparatusIntercellular Signaling Peptides and ProteinsMembrane FusionModels, BiologicalMolecular Sequence DataMultivesicular BodiesPeptidesPhagosomesQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsACB1 protein, S cerevisiaeCarrier ProteinsIntercellular Signaling Peptides and ProteinsPeptidesQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSDF-2 protein, Dictyostelium discoideumSSO1 protein, S cerevisiae

Identifiers

PMID20156967
PMCPMC2828925
OpenAlexW1993690543

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.