Evidence map›Paper›PMID 10866691›Full record

ArticleMolecular and cellular biology2000

Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane.

Y Feng, N G Davis

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.1field-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

48 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Protein Palmitoylation Plays an Important Role inMolecular & cellular proteomics : MCP · 2018
    Article
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  9. Article
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  11. Article
  12. Article
  13. Cu/Zn superoxide dismutase and the proton ATPase Pma1p of Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2015
    Article
  14. Article
  15. Mitochondrial protein import under kinase surveillance.Microbial cell (Graz, Austria) · 2014
    Review
  16. Article
  17. Review
  18. The glucose signaling network in yeast.Biochimica et biophysica acta · 2013
    Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Y FengDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
N G Davis
Wayne State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination of the plasma membrane-localized yeast a-factor receptor (Ste3p) triggers a rapid, ligand-independent endocytosis leading to its vacuolar degradation. This report identifies two mutants that block uptake by blocking ubiquitination, these being mutant either for the ankyrin repeat protein Akr1p or for the redundant type I casein kinases Yck1p and Yck2p. While no obvious defect was seen for wild-type Ste3p phosphorylation in akr1 or yck mutant backgrounds, examination of the Delta320-413 Ste3p deletion mutant phosphorylation did reveal a clear defect in both mutants. The Delta320-413 deletion removes 18 Ser-Thr residues (possible YCK-independent phosphorylation sites) yet retains the 15 Ser-Thr residues of the Ste3p PEST-like ubiquitination-endocytosis signal. Two other phenotypes link akr1 and yck mutants: both are defective in phosphorylation of wild-type alpha-factor receptor, and while both are defective for Ste3p constitutive internalization, both remain partially competent for the Ste3p ligand-dependent uptake mode. Yck1p-Yck2p may be the function responsible in phosphorylation of the PEST-like ubiquitination-endocytosis signal. Akr1p appears to function in localizing Yck1p-Yck2p to the plasma membrane, a localization that depends on prenylation of C-terminal dicysteinyl motifs. In akr1Delta cells, Yck2p is mislocalized, showing a diffuse cytoplasmic localization identical to that seen for a Yck2p mutant that lacks the C-terminal Cys-Cys, indicating a likely Akr1p requirement for the lipid modification of Yck2p, for prenylation, or possibly for palmitoylation.

Indexed as

EndocytosisReceptors, G-Protein-CoupledReceptors, PheromoneSaccharomyces cerevisiae ProteinsTranscription FactorsAcyltransferasesCasein KinasesCell MembraneCytoplasmFungal ProteinsMutationPhosphorylationProtein KinasesProtein PrenylationReceptors, Cell SurfaceReceptors, Mating FactorAcyltransferasesAKR1 protein, S cerevisiaeCasein KinasesFungal ProteinsProtein KinasesReceptors, Cell SurfaceReceptors, G-Protein-CoupledReceptors, Mating FactorReceptors, PeptideReceptors, PheromoneSaccharomyces cerevisiae ProteinsSTE3 protein, S cerevisiaeTranscription FactorsUbiquitins

Identifiers

PMID10866691
PMCPMC85984
OpenAlexW2100929292

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.