Evidence map›Paper›PMID 29738715›Full record

ArticleDevelopmental cell2018

Phosphorylation-Mediated Clearance of Amyloid-like Assemblies in Meiosis.

Kayla Carpenter, Rachel Brietta Bell, Julius Yunus, Angelika Amon, Luke Edwin Berchowitz

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 77 citations in OpenAlex.

  1. Rap1-mediated steric hindrance protects telomeres from MRX sensing.Nature structural & molecular biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Vir1p, the Yeast Homolog of Virilizer, is Required for mRNA mbioRxiv : the preprint server for biology · 2023
    Article
  17. Kar4 is Required for the Normal Pattern of Meiotic Gene Expression.bioRxiv : the preprint server for biology · 2023
    Article
  18. Kar4, the Yeast Homolog of METTL14, is Required for mRNA mbioRxiv : the preprint server for biology · 2023
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Kayla CarpenterDepartment of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, Hammer Health Sciences Building, Room 1520, New York, NY 10032, USA.
Rachel Brietta BellDepartment of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, Hammer Health Sciences Building, Room 1520, New York, NY 10032, USA.
Julius YunusDepartment of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, Hammer Health Sciences Building, Room 1520, New York, NY 10032, USA.
Angelika AmonKoch Institute for Integrative Cancer Biology, Massachusetts Institute of Technology, Cambridge, MA, USA; Howard Hughes Medical Institute, Chevy Chase, MD, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Luke Edwin BerchowitzDepartment of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, Hammer Health Sciences Building, Room 1520, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's and the Aging Brain, New York, NY, USA. Electronic address: leb2210@cumc.columbia.edu.
Columbia University Irving Medical Center · USHoward Hughes Medical Institute · US

Funding

Elucidation of regulation and function of amyloid-like assembliesR35GM124633 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Luke E Berchowitz · 2017 to 2026
$4.2M
Causes and consequences of aneuploidyR35GM118066 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI AMON, ANGELIKA B · 2016 to 2020
$1.9M
NIGMS NIH HHS R35 GM118066NIGMS NIH HHS R35 GM124633
6 · The paper itself

Abstract

Amyloids are fibrous protein assemblies that are often described as irreversible and intrinsically pathogenic. However, yeast cells employ amyloid-like assemblies of the RNA-binding protein Rim4 to control translation during meiosis. Here, we show that multi-site phosphorylation of Rim4 is critical for its regulated disassembly and degradation and that failure to clear Rim4 assemblies interferes with meiotic progression. Furthermore, we identify the protein kinase Ime2 to bring about Rim4 clearance via phosphorylation of Rim4's intrinsically disordered region. Rim4 phosphorylation leads to reversal of its amyloid-like properties and degradation by the proteasome. Our data support a model in which a threshold amount of phosphorylation, rather than modification of critical residues, is required for Rim4 clearance. Our results further demonstrate that at least some amyloid-like assemblies are not as irreversible as previously thought. We propose that the natural pathways by which cells process these structures could be deployed to act on disease-related amyloids.

Indexed as

Protein AggregatesAmyloidogenic ProteinsIntracellular Signaling Peptides and ProteinsMeiosisPhosphorylationProtein Serine-Threonine KinasesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidogenic ProteinsIME2 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsProtein AggregatesProtein Serine-Threonine KinasesRim4 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae Proteinsamyloid-like assembliesgametogenesismeiosisneurodegenerationphosphorylationRNA-binding proteinstranslation

Identifiers

PMID29738715
PMCPMC5944619
OpenAlexW2802277829

What OpenQuestion holds

Textmetadata
LicenceTDM
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.