Evidence map›Paper›PMID 23159559›Full record

ArticleJournal of molecular biology2013

A protein.protein interaction platform involved in recruitment of GLD-3 to the FBF.fem-3 mRNA complex.

Joann Wu, Zachary T Campbell, Elena Menichelli, Marvin Wickens, James R Williamson

Abstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

20 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A higher order PUF complex is central to regulation ofbioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Functional significance of PUF partnerships inbioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Sex Determination in Nematode Germ Cells.Sexual development : genetics, molecular biology, evolution, endocrinology, embryology, and pathology of sex determination and differentiation · 2022
    Review
  11. Review
  12. Review
  13. RNA control in pain: Blame it on the messenger.Wiley interdisciplinary reviews. RNA · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. RNA-binding proteins in pain.Wiley interdisciplinary reviews. RNA
    Review
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

5 authors at 2 institutions in 1 country.

Joann WuDepartment of Molecular Biology, Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Zachary T Campbell
Elena Menichelli
Marvin Wickens
James R Williamson
Scripps Research Institute · USUniversity of Wisconsin–Madison · US

Funding

FUNCTION OF POLY(A) AND 3'UTRSR01GM050942 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WICKENS, MARVIN P. · 1994 to 2020
$8.3M
NMR STUDIES OF THE HIV REV PEPITDE-RRE COMPLEXR01GM053320 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 1995 to 2010
$4.9M
Cleavage, polyadenylation, and transport of mRNAR37GM031892 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WICKENS, MARVIN P. · 2003 to 2012
$3.5M
CLEAVAGE, POLYADENYLATION, AND TRANSPORT OF MRNAR01GM031892 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI WICKENS, MARVIN P. · 1985 to 2000
$278k
Germline Regulation by PUF/CPEB Protein ComplexesF32GM095169 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CAMPBELL, ZACHARY · 2011 to 2012
$105k
NIGMS NIH HHS F32 GM095169NIGMS NIH HHS GM031892NIGMS NIH HHS GM050942NIGMS NIH HHS GM-53320NIGMS NIH HHS R01 GM031892NIGMS NIH HHS R01 GM050942NIGMS NIH HHS R01 GM053320NIGMS NIH HHS R37 GM031892
6 · The paper itself

Abstract

The Pumilio and FBF (PUF) family of RNA-binding proteins interacts with protein partners to post-transcriptionally regulate mRNAs in eukaryotes. The interaction between PUF family member fem-3 binding factor (FBF) and germline development defective-3 (GLD-3) protein promotes spermatogenesis in Caenorhabditis elegans by increasing expression of the fem-3 mRNA. Defined here in these studies is the molecular basis for this critical interaction. A 10-amino-acid region within GLD-3 is required for FBF binding, while a 7-amino-acid loop in FBF between PUF repeats 7 and 8 is necessary for GLD-3 binding. These short sequences are conserved, as other FBF-binding proteins bear sequences similar to those in GLD-3 and other C. elegans PUF proteins contain sequences similar to those in FBF. The FBF-binding region of GLD-3 forms a ternary complex with FBF on the point mutation element (PME) in the fem-3 3' untranslated region, and formation of this GLD-3⋅FBF complex does not impact the RNA-binding activity of FBF. These data raise the possibility of alternative models involving the formation of a GLD-3⋅FBF⋅RNA complex in the regulation of germline mRNAs.

Indexed as

Amino AcidsAmino Acid SequenceAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsElectrophoresis, Polyacrylamide GelElectrophoretic Mobility Shift AssayModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Interaction MappingProtein Structure, TertiaryRepetitive Sequences, Amino AcidRNA-Binding ProteinsAmino AcidsCaenorhabditis elegans Proteinsfem-3-binding protein, C elegansfem-3 protein, C elegansGLD-3 protein, C elegansRNA-Binding ProteinsRNA, HelminthRNA, Messenger

Identifiers

PMID23159559
PMCPMC3568228
OpenAlexW2076454210

What OpenQuestion holds

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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.