Evidence map›Paper›PMID 11287615›Full record

ArticleMolecular and cellular biology2001

Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast.

J M Galan, A Wiederkehr, J H Seol, R Haguenauer-Tsapis, R J Deshaies, H Riezman, M Peter

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

92 citing papers in PubMed.

  1. Article
  2. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  3. Review
  4. Article
  5. Review
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  18. Review
  19. Article
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32 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

7 authors.

J M GalanSwiss Institute for Experimental Cancer Research, 1066 Epalinges/VD, Switzerland.
A Wiederkehr
J H Seol
R Haguenauer-Tsapis
R J Deshaies
H Riezman
M Peter

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skp1p-cullin-F-box protein (SCF) complexes are ubiquitin-ligases composed of a core complex including Skp1p, Cdc53p, Hrt1p, the E2 enzyme Cdc34p, and one of multiple F-box proteins which are thought to provide substrate specificity to the complex. Here we show that the F-box protein Rcy1p is required for recycling of the v-SNARE Snc1p in Saccharomyces cerevisiae. Rcy1p localized to areas of polarized growth, and this polarized localization required its CAAX box and an intact actin cytoskeleton. Rcy1p interacted with Skp1p in vivo in an F-box-dependent manner, and both deletion of its F box and loss of Skp1p function impaired recycling. In contrast, cells deficient in Cdc53p, Hrt1p, or Cdc34p did not exhibit recycling defects. Unlike the case for F-box proteins that are known to participate in SCF complexes, degradation of Rcy1p required neither its F box nor functional 26S proteasomes or other SCF core subunits. Importantly, Skp1p was the only major partner that copurified with Rcy1p. Our results thus suggest that a complex composed of Rcy1p and Skp1p but not other SCF components may play a direct role in recycling of internalized proteins.

Indexed as

F-Box ProteinsSaccharomyces cerevisiae ProteinsBinding SitesDNA-Binding ProteinsFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMembrane ProteinsPeptide SynthasesR-SNARE ProteinsSaccharomyces cerevisiaeSKP Cullin F-Box Protein LigasesVesicular Transport ProteinsDNA-Binding ProteinsF-Box ProteinsFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMembrane ProteinsPeptide SynthasesRCY1 protein, S cerevisiaeR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSKP1 protein, S cerevisiaeSKP Cullin F-Box Protein LigasesSNC1 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID11287615
PMCPMC86938

What OpenQuestion holds

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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.