Evidence map›Paper›PMID 21777813›Full record

ArticleMolecular cell2011

Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton.

Tatiana A Chernova, Andrey V Romanyuk, Tatiana S Karpova, John R Shanks, Moiez Ali, Nela Moffatt, Rebecca L Howie, Andrew O'Dell, James G McNally, Susan W Liebman and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.7field-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

54 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein clearance strategies for disease intervention.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  6. Article
  7. Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. The three faces of Sup35.Yeast (Chichester, England) · 2019
    Review
  13. Article
  14. Article
  15. The Insoluble Protein Deposit (IPOD) in Yeast.Frontiers in molecular neuroscience · 2018
    Article
  16. Proteolysis suppresses spontaneous prion generation in yeast.The Journal of biological chemistry · 2017
    Article
  17. Article
  18. 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

12 authors at 4 institutions in 1 country.

Tatiana A ChernovaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Andrey V Romanyuk
Tatiana S Karpova
John R Shanks
Moiez Ali
Nela Moffatt
Rebecca L Howie
Andrew O'Dell
James G McNally
Susan W Liebman
Yury O Chernoff
Keith D Wilkinson
Emory University · USGeorgia Institute of Technology · USNational Cancer Institute · USUniversity of Illinois Chicago · US

Funding

YEAST PRION FACTOR (PSI+)R01GM056350 · NIGMS · UNIVERSITY OF NEVADA RENO · PI LIEBMAN, SUSAN W · 1997 to 2018
$6.6M
UBIQUITIN-DEPENDENT PROTEOLYSIS--SPECIFICITY/MECHANISMR01GM030308 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 1985 to 2010
$3.9M
GENETIC STUDY OF THE YEAST PRION INTERACTING PROTEINSR01GM058763 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI CHERNOFF, YURY O · 1999 to 2010
$2.6M
Functions of Ub-like Proteins &Processing ProteasesR01GM066355 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2002 to 2009
$2.5M
Fluorescence Imaging FacilityZICBC010571 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MCNALLY, JAMES G · 2009 to 2013
$1.3M
NIGMS NIH HHS GM56350NIGMS NIH HHS GM58763NIGMS NIH HHS R01 GM030308NIGMS NIH HHS R01 GM056350NIGMS NIH HHS R01 GM058763NIGMS NIH HHS R01 GM066355
6 · The paper itself

Abstract

Yeast prions are self-perpetuating, QN-rich amyloids that control heritable traits and serve as a model for mammalian amyloidoses. De novo prion formation by overproduced prion protein is facilitated by other aggregated QN-rich protein(s) and is influenced by alterations of protein homeostasis. Here we explore the mechanism by which the Las17-binding protein Lsb2 (Pin3) promotes conversion of the translation termination factor Sup35 into its prion form, [PSI(+)]. We show that Lsb2 localizes with some Sup35 aggregates and that Lsb2 is a short-lived protein whose levels are controlled via the ubiquitin-proteasome system and are dramatically increased by stress. Loss of Lsb2 decreases stability of [PSI(+)] after brief heat shock. Mutations interfering with Lsb2 ubiquitination increase prion induction, while a mutation eliminating association of Lsb2 with the actin cytoskeleton blocks its aggregation and prion-inducing ability. These findings directly implicate the UPS and actin cytoskeleton in regulating prions via a stress-inducible QN-rich protein.

Indexed as

ActinsCarrier ProteinsCytoskeletonMutationPeptide Termination FactorsPrionsProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalUbiquitinationActinsCarrier Proteinslas17-binding protein Lsb2, S cerevisiaePeptide Termination FactorsPrionsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID21777813
PMCPMC3151368
OpenAlexW2054393791

What OpenQuestion holds

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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.