Evidence map›Paper›PMID 15012629›Full record

ArticleThe Biochemical journal2004

Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes.

Sonja Baum, Margarethe Bittins, Steffen Frey, Matthias Seedorf

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

60 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Local translation of yeastRNA (New York, N.Y.) · 2019
    Article
  11. Article
  12. RACK1 on and off the ribosome.RNA (New York, N.Y.) · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017
    Article
  17. Article
  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

4 authors at 1 institution in 1 country.

Sonja BaumCenter of Molecular Biology at University of Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany.
Margarethe Bittins
Steffen Frey
Matthias Seedorf
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scp160p interacts in an mRNA-dependent manner with translating ribosomes via multiple RNA-binding heterogeneous nuclear ribonucleoprotein K-homology (KH) domains. In the present study, we show by protein-protein cross-linking that Scp160p is in close proximity to translation elongation factor 1A and the WD40 (Trp-Asp 40)-repeat containing protein Asc1p at ribosomes. Analysis of a truncation mutant revealed that the C-terminus of Scp160p is essential for ribosome binding and that Cys(1067) at the C-terminus of Scp160p is required to obtain these cross-links. The interaction of Scp160p with ribosomes depends on Asc1p. In fast-growing yeast cells, nearly all Asc1p is tightly bound to ribosomes, but it can also be present in a ribosome-free form depending on growth conditions. The functional homologue of Asc1p, mammalian RACK1 (receptor of activated C kinase), was previously characterized as an adaptor protein bridging activated signalling molecules with their substrates. Our results suggest that Scp160p connects specific mRNAs, ribosomes and a translation factor with an adaptor for signalling molecules. These interactions might regulate the translation activity of ribosomes programmed with specific mRNAs.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCross-Linking ReagentsElectrophoretic Mobility Shift AssayGTP-Binding ProteinsMembrane ProteinsMutationNuclear ProteinsPeptide Elongation Factor 1PeptidesPolyribosomesProtein Structure, TertiaryRibosomesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportASC1 protein, S cerevisiaeCross-Linking ReagentsGTP-Binding ProteinsMembrane ProteinsNuclear ProteinsPeptide Elongation Factor 1PeptidesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSCP160 protein, S cerevisiae

Identifiers

PMID15012629
PMCPMC1224212
OpenAlexW2119600052

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.