Evidence map›Paper›PMID 11867544›Full record

ArticleThe EMBO journal2002

The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast.

Kenji Irie, Tomofumi Tadauchi, Peter A Takizawa, Ronald D Vale, Kunihiro Matsumoto, Ira Herskowitz

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

61 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Identification of RNA-Binding Protein Targets with HyperTRIBE inInternational journal of molecular sciences · 2023
    Article
  5. Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022
    Article
  6. Expression of a homologue of a vertebrate non-visual opsin Opn3 in the insect photoreceptors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Article
  18. Article
  19. Article
  20. Principles of mRNA transport in yeast.Cellular and molecular life sciences : CMLS · 2012
    Review

1 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 2 countries.

Kenji IrieDepartment of Molecular Biology, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Tomofumi Tadauchi
Peter A Takizawa
Ronald D Vale
Kunihiro Matsumoto
Ira Herskowitz
Japan Science and Technology Agency · JP

Funding

MICROTUBULE-BASED ORGANELLE TRANSPORTR01GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI VALE, RONALD D · 1988 to 2005
$1.2M
NIGMS NIH HHS R01 GM038499
6 · The paper itself

Abstract

RNA localization is a widespread mechanism for achieving localized protein synthesis. In Saccharomyces cerevisiae, Ash1 is a specific repressor of transcription that localizes asymmetrically to the daughter cell nucleus through the localization of ASH1 mRNA to the distal tip of the daughter cell. This localization depends on the actin cytoskeleton and five She proteins, one of which is a type V myosin motor, Myo4. We show here that a novel RNA-binding protein, Khd1 (KH-domain protein 1), is required for efficient localization of ASH1 mRNA to the distal tip of the daughter cell. Visualization of ASH1 mRNA in vivo using GFP-tagged RNA demonstrated that Khd1 associates with the N element, a cis-acting localization sequence within the ASH1 mRNA. Co-immunoprecipitation studies also indicated that Khd1 associates with ASH1 mRNA through the N element. A khd1Delta mutation exacerbates the phenotype of a weak myo4 mutation, whereas overexpression of KHD1 decreases the concentration of Ash1 protein and restores HO expression to she mutants. These results suggest that Khd1 may function in the linkage between ASH1 mRNA localization and its translation.

Indexed as

DNA-Binding ProteinsRepressor ProteinsAmino Acid MotifsBinding SitesCell PolarityCytoskeletonDeoxyribonucleases, Type II Site-SpecificMacromolecular SubstancesMolecular Motor ProteinsPhenotypeProtein BiosynthesisProtein Interaction MappingProto-Oncogene ProteinsRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidRibonucleoproteinsASH1 protein, S cerevisiaeDeoxyribonucleases, Type II Site-SpecificDNA-Binding ProteinsHEK2 protein, S cerevisiaeHO protein, S cerevisiaeMacromolecular SubstancesMolecular Motor ProteinsProto-Oncogene ProteinsRecombinant Fusion ProteinsRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSCEI protein, S cerevisiaeShe protein, mouseTranscription Factors

Identifiers

PMID11867544
PMCPMC125877
OpenAlexW2104514904

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.