Evidence map›Paper›PMID 14561888›Full record

ArticleRNA (New York, N.Y.)2003

RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex.

Graydon B Gonsalvez, Katrina A Lehmann, Derek K Ho, Eleni S Stanitsa, James R Williamson, Roy M Long

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Cellular and molecular mechanisms of asymmetric stem cell division in tissue homeostasis.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Structure of a myosin•adaptor complex and pairing by cargo.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. mRNA trafficking in fungi.Molecular genetics and genomics : MGG · 2007
    Review
  18. Article
  19. Article
  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

6 authors at 2 institutions in 1 country.

Graydon B GonsalvezDepartment of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
Katrina A Lehmann
Derek K Ho
Eleni S Stanitsa
James R Williamson
Roy M Long
Medical College of Wisconsin · USScripps Research Institute · US

Funding

NMR STUDIES OF THE HIV REV PEPITDE-RRE COMPLEXR01GM053320 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 1995 to 2010
$4.9M
RNA LOCALIZATION IN S.CEREVISIAER01GM060392 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI LONG, ROY M · 2000 to 2004
$1.1M
ASH1 mRNA pre-localizaton ribonucleoprotein assemblyF32GM065718 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI LEHMANN, KATRINA A · 2002 to 2003
$85k
NIGMS NIH HHS F32 GM065718NIGMS NIH HHS GM60392NIGMS NIH HHS GM65718NIGMS NIH HHS R01 GM053320NIGMS NIH HHS R01 GM060392
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, ASH1 mRNA is localized to the tip of daughter cells during anaphase of the cell cycle. ASH1 mRNA localization is dependent on four cis-acting localization elements as well as Myo4p, She2p, and She3p. Myo4p, She2p, and She3p are hypothesized to form a heterotrimeric protein complex that directly transports ASH1 mRNA to daughter cells. She2p is an RNA-binding protein that directly interacts with ASH1 cis-acting localization elements and associates with She3p. Here we report the identification of seven She2p mutants-N36S, R43A, R44A, R52A, R52K, R63A, and R63K-that result in the delocalization of ASH1 mRNA. These mutants are defective for RNA-binding activity but retain the ability to interact with She3p, indicating that a functional She2p RNA-binding domain is not a prerequisite for association with She3p. Furthermore, the nuclear/cytoplasmic distribution for the N36S and R63K She2p mutants is not altered, indicating that nuclear/cytoplasmic trafficking of She2p is independent of RNA-binding activity. Using the N36S and R63K She2p mutants, we observed that in the absence of She2p RNA-binding activity, neither Myo4p nor She3p is asymmetrically sorted to daughter cells. However, in the absence of She2p, Myo4p and She3p can be asymmetrically segregated to daughter cells by artificially tethering mRNA to She3p, implying that the transport and/or anchoring of the Myo4p/She3p complex is dependent on the presence of associated mRNA.

Indexed as

DNA-Binding ProteinsPoint MutationPrecipitin TestsProtein BindingRepressor ProteinsReverse Transcriptase Polymerase Chain ReactionRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsTranscription FactorsTwo-Hybrid System TechniquesASH1 protein, S cerevisiaeDNA-Binding ProteinsIST2 protein, S cerevisiaeRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID14561888
PMCPMC1287060
OpenAlexW2096144054

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.