Evidence map›Paper›PMID 15973437›Full record

ArticleThe EMBO journal2005

Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation.

Javier Valdez-Taubas, Hugh Pelham

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

97 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
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  8. Article
  9. Article
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  11. Ubiquitin-mediated degradation at the Golgi apparatus.Frontiers in molecular biosciences · 2023
    Review
  12. Review
  13. Chemical Synthesis and Semisynthesis of Lipidated Proteins.Angewandte Chemie (International ed. in English) · 2022
    Review
  14. Chemische Synthese und Semisynthese von lipidierten Proteinen.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Review
  15. Article
  16. Review
  17. The Many Faces of Lipids in Genome Stability (and How to Unmask Them).International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. Article

37 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.

Javier Valdez-TaubasMRC Laboratory of Molecular Biology, Cambridge, UK.
Hugh Pelham
MRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein palmitoylation is a post-translational modification that affects a great number of proteins. In most cases, the enzymes responsible for this modification have not been identified. Some proteins use palmitoylation to attach themselves to membranes; however, palmitoylation also occurs in transmembrane proteins, and the function of this palmitoylation is less clear. Here we identify Swf1, a member of the DHHC-CDR family of palmitoyltransferases, as the protein responsible for modifying the yeast SNAREs Snc1, Syn8 and Tlg1, at cysteine residues close to the cytoplasmic end of their single transmembrane domains (TMDs). In an swf1Delta mutant, Tlg1 is mis-sorted to the vacuole. This occurs because unpalmitoylated Tlg1 is recognised by the ubiquitin ligase Tul1, resulting in its targeting to the multivesicular body pathway. Our results suggest that one role of palmitoylation is to protect TMDs from the cellular quality control machinery, and that Swf1 may be the enzyme responsible for most, if not all, TMD-associated palmitoylation in yeast.

Indexed as

AcyltransferasesAmino Acid SequenceCarnitine O-PalmitoyltransferaseEndoplasmic ReticulumGenes, ReporterHumansMembrane ProteinsMolecular Sequence DataPalmitic AcidR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomycesSNARE ProteinsUbiquitinUbiquitin-Protein LigasesVesicular Transport ProteinsAcyltransferasesCarnitine O-PalmitoyltransferaseMembrane ProteinsPalmitic AcidR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSNC1 protein, S cerevisiaeSwf1 protein, S cerevisiaeTlg1 protein, S cerevisiaeTUL1 protein, S cerevisiaeUbiquitinUbiquitin-Protein LigasesVesicular Transport Proteins

Identifiers

PMID15973437
PMCPMC1176453
OpenAlexW2100139095

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.