Evidence map›Paper›PMID 28139700›Full record

ArticleScientific reports2017

The crystal structure of the Sgt1-Skp1 complex: the link between Hsp90 and both SCF E3 ubiquitin ligases and kinetochores.

Oliver Willhoft, Richard Kerr, Dipali Patel, Wenjuan Zhang, Caezar Al-Jassar, Tina Daviter, Stefan H Millson, Konstantinos Thalassinos, Cara K Vaughan

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Effects of theFrontiers in plant science · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

9 authors at 4 institutions in 1 country.

Oliver WillhoftInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
Richard KerrInstitute of Structural and Molecular Biology, University College London and Birkbeck, Division of Biosciences, Darwin Building, Gower Street, London, WC1E 6BT, UK.
Dipali PatelInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
Wenjuan ZhangInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
Caezar Al-JassarInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
Tina DaviterInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
Stefan H MillsonSchool of Life Sciences, Joseph Banks Laboratory, University of Lincoln, Lincoln, LN6 7TS, UK.
Konstantinos ThalassinosInstitute of Structural and Molecular Biology, University College London and Birkbeck, Division of Biosciences, Darwin Building, Gower Street, London, WC1E 6BT, UK.
Cara K VaughanInstitute of Structural and Molecular Biology, University College London and Birkbeck, Biological Sciences, Malet Street, London, WC1E 7HX, UK.
University College London · GBBirkbeck, University of London · GBInstitute of Structural and Molecular Biology · GBUniversity of Lincoln · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The essential cochaperone Sgt1 recruits Hsp90 chaperone activity to a range of cellular factors including SCF E3 ubiquitin ligases and the kinetochore in eukaryotes. In these pathways Sgt1 interacts with Skp1, a small protein that heterodimerizes with proteins containing the F-box motif. We have determined the crystal structure of the interacting domains of Saccharomyces cerevisiae Sgt1 and Skp1 at 2.8 Å resolution and validated the interface in the context of the full-length proteins in solution. The BTB/POZ domain of Skp1 associates with Sgt1 via the concave surface of its TPR domain using residues that are conserved in humans. Dimerization of yeast Sgt1 occurs via an insertion that is absent from monomeric human Sgt1. We identify point mutations that disrupt dimerization and Skp1 binding in vitro and find that the interaction with Skp1 is an essential function of Sgt1 in yeast. Our data provide a structural rationale for understanding the phenotypes of temperature-sensitive Sgt1 mutants and for linking Skp1-associated proteins to Hsp90-dependent pathways.

Indexed as

Models, MolecularProtein ConformationAdaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesConserved SequenceF-Box ProteinsHSP90 Heat-Shock ProteinsKinetochoresProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationRecombinant ProteinsSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesAdaptor Proteins, Signal TransducingF-Box ProteinsHSP90 Heat-Shock ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSGT1 protein, S cerevisiaeSKP1 protein, S cerevisiaeSKP Cullin F-Box Protein Ligases

Identifiers

PMID28139700
PMCPMC5282575
OpenAlexW2584768285

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.