Evidence map›Paper›PMID 23045389›Full record

ArticleMolecular and cellular biology2012

Regulation of chaperone effects on a yeast prion by cochaperone Sgt2.

Denis A Kiktev, Jesse C Patterson, Susanne Müller, Bhawana Bariar, Tao Pan, Yury O Chernoff

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Multiomics ofInternational journal of molecular sciences · 2023
    Article
  3. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Heat shock protein 104 (Hsp104)-mediated curing of [The Journal of biological chemistry · 2017
    Article
  16. Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    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

6 authors at 1 institution in 1 country.

Denis A KiktevSchool of Biology and Parker H. Petit Institute for Bioengineering & Bioscience, Georgia Institute of Technology, Atlanta, Georgia, USA.
Jesse C Patterson
Susanne Müller
Bhawana Bariar
Tao Pan
Yury O Chernoff
Georgia Institute of Technology · US

Funding

GENETIC STUDY OF THE YEAST PRION INTERACTING PROTEINSR01GM058763 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI CHERNOFF, YURY O · 1999 to 2010
$2.6M
Ubiquitin and regulation of prion induction by a short-lived proteinR01GM093294 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2011 to 2014
$1.3M
NIGMS NIH HHS R01 GM058763NIGMS NIH HHS R01GM058763NIGMS NIH HHS R01 GM093294NIGMS NIH HHS R01GM093294
6 · The paper itself

Abstract

Yeast prions, based on self-seeded highly ordered fibrous aggregates (amyloids), serve as a model for human amyloid diseases. Propagation of yeast prions depends on the balance between chaperones of the Hsp100 and Hsp70 families. The yeast prion [PSI(+)] can be eliminated by an excess of the chaperone Hsp104. This effect is reversed by an excess of the chaperone Hsp70-Ssa. Here we show that the actions of Hsp104 and Ssa on [PSI(+)] are modulated by the small glutamine-rich tetratricopeptide cochaperone Sgt2. Sgt2 is conserved from yeast to humans, has previously been implicated in the guided entry of tail-anchored proteins (GET) trafficking pathway, and is known to interact with Hsps, cytosolic Get proteins, and tail-anchored proteins. We demonstrate that Sgt2 increases the ability of excess Ssa to counteract [PSI(+)] curing by excess Hsp104. Deletion of SGT2 also restores trafficking of a tail-anchored protein in cells with a disrupted GET pathway. One region of Sgt2 interacts both with the prion domain of Sup35 and with tail-anchored proteins. Sgt2 levels are increased in response to the presence of a prion when major Hsps are not induced. Our data implicate Sgt2 as an amyloid "sensor" and a regulator of chaperone targeting to different types of aggregation-prone proteins.

Indexed as

Adaptor Proteins, Vesicular TransportCarrier ProteinsGene DeletionGenes, FungalHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansModels, BiologicalMolecular ChaperonesPeptide Termination FactorsProtein MultimerizationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Vesicular TransportCarrier ProteinsGet2 protein, S cerevisiaeHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptide Termination FactorsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSgt2 protein, S cerevisiaeSSA3 protein, S cerevisiaeSUP35 protein, S cerevisiae

Identifiers

PMID23045389
PMCPMC3510541
OpenAlexW2081233603

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.