Evidence map›Paper›PMID 15044687›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation.

Masayoshi Fukasawa, Oleg Varlamov, William S Eng, Thomas H Söllner, James E Rothman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

70 citing papers in PubMed, 152 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. ELAPOR1 is a copper-dependent tethering factor driving proacrosomal vesicle fusion during acrosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Article
  8. Alpha-Synuclein Inhibits the Secretion of Extracellular Vesicles through Disruptions in YKT6 Lipidation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  9. Article
  10. Article
  11. α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson's disease.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  12. Article
  13. Article
  14. The role of syntaxins in retinal function and health.Frontiers in cellular neuroscience · 2024
    Review
  15. Article
  16. Cell biology of protein-lipid conjugation.Cell structure and function · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

10 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

5 authors at 1 institution in 1 country.

Masayoshi FukasawaCellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Oleg Varlamov
William S Eng
Thomas H Söllner
James E Rothman
Memorial Sloan Kettering Cancer Center · US

Funding

Regulation of Membrane Fusion in ExocytosisR01DK027044 · NIDDK · YALE UNIVERSITY · PI KRISHNAKUMAR, SHYAM S · 1986 to 2021
$8.2M
NIDDK NIH HHS 5 R01 DK27044NIDDK NIH HHS R01 DK027044
6 · The paper itself

Abstract

Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) catalyze compartment-specific membrane fusion. Whereas most SNAREs are bona fide type II membrane proteins, Ykt6 lacks a proteinaceous membrane anchor but contains a prenylation consensus motif (CAAX box) and exists in an inactive cytosolic and an active membrane-bound form. We demonstrate that both forms are farnesylated at the carboxyl-terminal cysteine of the CCAIM sequence. Farnesylation is the prerequisite for subsequent palmitoylation of the upstream cysteine, which permits stable membrane association of Ykt6. The double-lipid modification and membrane association is crucial for intra-Golgi transport in vitro and cell homeostasis/survival in vivo. The membrane recruitment and palmitoylation is controlled by the N-terminal domain of Ykt6, which interacts with the SNARE motif, keeping it in an inactive closed conformation. Together, these results suggest that conformational changes control the lipid modification and function of Ykt6. Considering the essential and central role of Ykt6 in the secretory pathway, this spatial and functional cycle might provide a mechanism to regulate the rate of intracellular membrane flow.

Indexed as

Vesicular Transport ProteinsCytosolMembrane ProteinsMicroscopy, FluorescencePalmitic AcidPlasmidsSNARE ProteinsMembrane ProteinsPalmitic AcidSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID15044687
PMCPMC387331
OpenAlexW2013329798

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.