Evidence map›Paper›PMID 18818696›Full record

ArticleThe EMBO journal2008

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes.

Minghao Zhang, Marta Botër, Kuoyu Li, Yasuhiro Kadota, Barry Panaretou, Chrisostomos Prodromou, Ken Shirasu, Laurence H Pearl

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Hsp90: A means to an end.Cell stress & chaperones · 2026
    Review
  3. Review
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  5. Identification of thePlants (Basel, Switzerland) · 2025
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  7. Review
  8. Article
  9. Article
  10. Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023
    Review
  11. FBXO38 Ubiquitin Ligase Controls Centromere Integrity via ZXDA/B Stability.Frontiers in cell and developmental biology · 2022
    Article
  12. Article
  13. Review
  14. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  15. Genome-wide analysis ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2020
    Article
  16. Article
  17. Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019
    Review
  18. Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019
    Article
  19. Article
  20. 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

8 authors at 5 institutions in 3 countries.

Minghao ZhangSection of Structural Biology, The Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
Marta Botër
Kuoyu Li
Yasuhiro Kadota
Barry Panaretou
Chrisostomos Prodromou
Ken Shirasu
Laurence H Pearl
Institute of Cancer Research · GBKing's College London · GBRIKEN Center for Sustainable Resource Science · JPBalfour Beatty (United Kingdom) · GBJohn Innes Centre · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Sgt1 is an adaptor protein implicated in a variety of processes, including formation of the kinetochore complex in yeast, and regulation of innate immunity systems in plants and animals. Sgt1 has been found to associate with SCF E3 ubiquitin ligases, the CBF3 kinetochore complex, plant R proteins and related animal Nod-like receptors, and with the Hsp90 molecular chaperone. We have determined the crystal structure of the core Hsp90-Sgt1 complex, revealing a distinct site of interaction on the Hsp90 N-terminal domain. Using the structure, we developed mutations in Sgt1 interfacial residues, which specifically abrogate interaction with Hsp90, and disrupt Sgt1-dependent functions in vivo, in plants and yeast. We show that Sgt1 bridges the Hsp90 molecular chaperone system to the substrate-specific arm of SCF ubiquitin ligase complexes, suggesting a role in SCF assembly and regulation, and providing multiple complementary routes for ubiquitination of Hsp90 client proteins.

Indexed as

Adaptor Proteins, Signal TransducingHSP90 Heat-Shock ProteinsModels, BiologicalMolecular ChaperonesMolecular ConformationNicotianaPlasmidsPoint MutationProtein BindingProtein ConformationProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityUbiquitinAdaptor Proteins, Signal TransducingHSP90 Heat-Shock ProteinsMolecular ChaperonesRepressor ProteinsSaccharomyces cerevisiae ProteinsSGT1 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID18818696
PMCPMC2556094
OpenAlexW2043244176

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.