Evidence map›Paper›PMID 15723044›Full record

ArticleEMBO reports2005

The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion.

Lars E P Dietrich, Karolina Peplowska, Tracy J LaGrassa, Haitong Hou, Jan Rohde, Christian Ungermann

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Cell biology of protein-lipid conjugation.Cell structure and function · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A lipid-anchored SNARE supports membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Article
  13. Article
  14. Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  15. Article
  16. Article
  17. Review
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

6 authors at 1 institution in 1 country.

Lars E P DietrichBiochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Karolina Peplowska
Tracy J LaGrassa
Haitong Hou
Jan Rohde
Christian Ungermann
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The farnesylated SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) Ykt6 mediates protein palmitoylation at the yeast vacuole by means of its amino-terminal longin domain. Ykt6 is localized equally to membranes and the cytosol, although it is unclear how this distribution is mediated. We now show that Ykt6 is released efficiently from vacuoles during an early stage of yeast vacuole fusion. This release is dependent on the disassembly of vacuolar SNAREs (priming). In recent literature, it had been demonstrated for mammalian Ykt6 that the membrane-bound form is both palmitoylated and farnesylated at its carboxy-terminal CAAX box, whereas soluble Ykt6 is only farnesylated. In agreement with this, we find that yeast Ykt6 becomes palmitoylated in vitro at its C-terminal CAAX motif. Mutagenesis of the potential palmitoylation site in yeast Ykt6 prevents stable membrane association and is lethal. On the basis of these and other findings, we speculate that Ykt6 is released from membranes by depalmitoylation. Such a mechanism could enable recycling of this lipid-anchored SNARE from the vacuole independent of retrograde transport.

Indexed as

Membrane FusionIntracellular MembranesMembrane ProteinsModels, MolecularMutationPalmitic AcidProtein Structure, TertiaryR-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsTime FactorsVacuolesVesicular Transport ProteinsMembrane ProteinsPalmitic AcidR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport ProteinsYKT6 protein, S cerevisiae

Identifiers

PMID15723044
PMCPMC1299260
OpenAlexW2105209462

What OpenQuestion holds

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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.