Evidence map›Paper›PMID 25143386›Full record

ArticleThe Journal of biological chemistry2014

Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion.

Moiez Ali, Tatiana A Chernova, Gary P Newnam, Luming Yin, John Shanks, Tatiana S Karpova, Andrew Lee, Oskar Laur, Sindhu Subramanian, Dami Kim and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Frontiers in molecular biosciences · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    Review
  13. Article
  14. Review
  15. Article
  16. 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

14 authors at 4 institutions in 2 countries.

Moiez AliFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Tatiana A ChernovaFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, tcherno@emory.edu.
Gary P Newnamthe School of Biology and Parker H. Petit Institute for Bioengineering & Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332.
Luming YinFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
John ShanksFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Tatiana S Karpovathe Center for Cancer Research Core Fluorescence Imaging Facility, Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Andrew LeeFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Oskar Laurthe Division of Microbiology, Yerkes Research Center, Emory University, Atlanta, Georgia 30329, and.
Sindhu SubramanianFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Dami KimFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
James G McNallythe Center for Cancer Research Core Fluorescence Imaging Facility, Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Nicholas T SeyfriedFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Yury O Chernoffthe School of Biology and Parker H. Petit Institute for Bioengineering & Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332, the Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg, Russia 199034.
Keith D WilkinsonFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, genekdw@emory.edu.
Emory University · USGeorgia Institute of Technology · USCenter for Cancer Research · USNational Cancer Institute · US

Funding

LRBGE Optical Microscopy CoreZICBC011574 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KARPOVA, TATIANA · 2014 to 2025
$7.4M
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 GM093294NIGMS NIH HHS R01 GM093294
6 · The paper itself

Abstract

Yeast prions are self-propagating amyloid-like aggregates of Q/N-rich protein that confer heritable traits and provide a model of mammalian amyloidoses. [PSI(+)] is a prion isoform of the translation termination factor Sup35. Propagation of [PSI(+)] during cell division under normal conditions and during the recovery from damaging environmental stress depends on cellular chaperones and is influenced by ubiquitin proteolysis and the actin cytoskeleton. The paralogous yeast proteins Lsb1 and Lsb2 bind the actin assembly protein Las17 (a yeast homolog of human Wiskott-Aldrich syndrome protein) and participate in the endocytic pathway. Lsb2 was shown to modulate maintenance of [PSI(+)] during and after heat shock. Here, we demonstrate that Lsb1 also regulates maintenance of the Sup35 prion during and after heat shock. These data point to the involvement of Lsb proteins in the partitioning of protein aggregates in stressed cells. Lsb1 abundance and cycling between actin patches, endoplasmic reticulum, and cytosol is regulated by the Guided Entry of Tail-anchored proteins pathway and Rsp5-dependent ubiquitination. Heat shock-induced proteolytic processing of Lsb1 is crucial for prion maintenance during stress. Our findings identify Lsb1 as another component of a tightly regulated pathway controlling protein aggregation in changing environments.

Indexed as

Heat-Shock ResponseActinsCarrier ProteinsCytoskeletonPeptide Termination FactorsPrionsProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCarrier ProteinsLsb1 protein, S cerevisiaePeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeActinEndoplasmic Reticulum (ER)Heat ShockPrionProteasomeRsp5Sup35Ubiquitylation (Ubiquitination)

Identifiers

PMID25143386
PMCPMC4183801
OpenAlexW2044061340

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.