Evidence map›Paper›PMID 31399582›Full record

ArticleNature communications2019

The prion-like protein kinase Sky1 is required for efficient stress granule disassembly.

Jenifer E Shattuck, Kacy R Paul, Sean M Cascarina, Eric D Ross

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. A novel SATB1 protein isoform with different biophysical properties.Frontiers in cell and developmental biology · 2023
    Article
  7. Article
  8. Protein interactions: anything new?Essays in biochemistry · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

Jenifer E ShattuckDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523, USA.
Kacy R PaulDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523, USA.ORCID http://orcid.org/0000-0002-9495-183X
Sean M CascarinaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523, USA.ORCID http://orcid.org/0000-0002-3054-2332
Eric D RossDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523, USA. eric.ross@colostate.edu.ORCID http://orcid.org/0000-0002-6473-9977
Colorado State University · USBoston University · US

Funding

Functional and Pathological Assembly of Prion-like DomainsR35GM130352 · NIGMS · COLORADO STATE UNIVERSITY · PI Eric D Ross · 2019 to 2026
$3.1M
NIGMS NIH HHS R35 GM130352
6 · The paper itself

Abstract

Stress granules are membraneless protein- and mRNA-rich organelles that form in response to perturbations in environmental conditions. Stress granule formation is reversible, and persistent stress granules have been implicated in a variety of neurodegenerative disorders, including amyotrophic lateral sclerosis. However, characterization of the factors involved in dissolving stress granules is incomplete. Many stress granule proteins contain prion-like domains (PrLDs), some of which have been linked to stress granule formation. Here, we demonstrate that the PrLD-containing yeast protein kinase Sky1 is a stress granule component. Sky1 is recruited to stress granules in part via its PrLD, and Sky1's kinase activity regulates timely stress granule disassembly during stress recovery. This effect is mediated by phosphorylation of the stress granule component Npl3. Sky1 can compensate for defects in chaperone-mediated stress granule disassembly and vice-versa, demonstrating that cells have multiple overlapping mechanisms for re-solubilizing stress granule components.

Indexed as

OrganellesPrionsProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGene Expression Regulation, FungalHeat-Shock ProteinsNeurodegenerative DiseasesNuclear ProteinsPhosphorylationPoly(A)-Binding ProteinsProtein DomainsRNA-Binding ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeNPL3 protein, S cerevisiaeNuclear Proteinspab1 protein, S cerevisiaePoly(A)-Binding ProteinsPrionsProtein Serine-Threonine KinasesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSKY1 protein, S cerevisiae

Identifiers

PMID31399582
PMCPMC6688984
OpenAlexW2968899732

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.