Evidence map›Paper›PMID 24981173›Full record

ArticleMolecular cell2014

Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.

Xiang Li, Joseph B Rayman, Eric R Kandel, Irina L Derkatch

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022
    Article
  11. ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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.

Xiang LiDepartment of Neuroscience, College of Physicians and Surgeons of Columbia University, 645 Kolb Research Annex, 1051 Riverside Drive, New York, NY 10032, USA.
Joseph B RaymanDepartment of Neuroscience, College of Physicians and Surgeons of Columbia University, 645 Kolb Research Annex, 1051 Riverside Drive, New York, NY 10032, USA.
Eric R KandelDepartment of Neuroscience, College of Physicians and Surgeons of Columbia University, 645 Kolb Research Annex, 1051 Riverside Drive, New York, NY 10032, USA; Department of Psychiatry, College of Physicians and Surgeons of Columbia University, New York State Psychiatric Institute, New York, NY 10032, USA; Kavli Institute for Brain Science, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA. Electronic address: erk5@columbia.edu.
Irina L DerkatchDepartment of Neuroscience, College of Physicians and Surgeons of Columbia University, 645 Kolb Research Annex, 1051 Riverside Drive, New York, NY 10032, USA. Electronic address: irina.derkatch@gmail.com.

Funding

Investigation of the Establishment of the Prion StateR01GM070934 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DERKATCH, IRINA L · 2006 to 2010
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS 7 R01 GM070934-06NIGMS NIH HHS R01 GM070934
6 · The paper itself

Abstract

Tia1/Pub1 is a stress granule component carrying a Q/N-rich prion domain. We provide direct evidence that Tia1 forms a prion in yeast. Moreover, Tia1/Pub1 acts cooperatively with release factor Sup35/eRF3 to establish a two-protein self-propagating state. This two-protein prion driven by the Q/N-rich prion domains of Sup35 and Tia1/Pub1 can be visualized as distinctive line structures along tubulin cytoskeleton. Furthermore, we find that tubulin-associated complex containing Pub1 and Sup35 oligomers normally exists in yeast, and its assembly depends on prion domains of Pub1 and Sup35. This Sup35/Pub1 complex, which also contains TUB1 mRNA and components of translation machinery, is important for the integrity of the tubulin cytoskeleton: PUB1 disruption and Sup35 depletion from the complex lead to cytoskeletal defects. We propose that the complex is implicated in protein synthesis at the site of microtubule assembly. Thus our study identifies the role for prion domains in the assembly of multiprotein complexes.

Indexed as

AmyloidAnimalsCytoskeletonMiceMice, Inbred C57BLPeptide Termination FactorsPoly(A)-Binding ProteinsPrionsProtein BiosynthesisProtein MultimerizationProtein Structure, TertiaryRecombinant ProteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiaeAmyloidpeptide-chain-release factor 3Peptide Termination FactorsPoly(A)-Binding ProteinsPrionsPUB1 protein, S cerevisiaeRecombinant ProteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeT-Cell Intracellular Antigen-1Tia1 protein, mouseTub1 protein, S cerevisiae

Identifiers

PMID24981173
PMCPMC4425694

What OpenQuestion holds

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Registered trials

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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.