Evidence map›Paper›PMID 21278383›Full record

ArticleThe Journal of biological chemistry2011

Molecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7A.

Batiste Boëda, Phillip P Knowles, David C Briggs, Judith Murray-Rust, Erika Soriano, Boyan K Garvalov, Neil Q McDonald, Michael Way

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Biallelic mutations inLife medicine · 2023
    Article
  4. A novel homozygous mutation in ACTL7A leads to male infertility.Molecular genetics and genomics : MGG · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Disruption inScience advances · 2020
    Article
  10. Article
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Testin on Atherosclerosis in Rabbits.Chinese medical journal · 2015
    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

8 authors at 5 institutions in 4 countries.

Batiste BoëdaCell Motility Laboratory, Cancer Research UK, London Research Institute, London, United Kingdom.
Phillip P Knowles
David C Briggs
Judith Murray-Rust
Erika Soriano
Boyan K Garvalov
Neil Q McDonald
Michael Way
Cancer Research UK · GBBirkbeck, University of London · GBJustus-Liebig-Universität Gießen · DEMotility (United States) · USThe Honourable Society of Lincoln's Inn · GB

Funding

Cancer Research UK 10747
6 · The paper itself

Abstract

Actin-related proteins (Arps) are a highly conserved family of proteins that have extensive sequence and structural similarity to actin. All characterized Arps are components of large multimeric complexes associated with chromatin or the cytoskeleton. In addition, the human genome encodes five conserved but largely uncharacterized "orphan" Arps, which appear to be mostly testis-specific. Here we show that Arp7A, which has 43% sequence identity with β-actin, forms a complex with the cytoskeletal proteins Tes and Mena in the subacrosomal layer of round spermatids. The N-terminal 65-residue extension to the actin-like fold of Arp7A interacts directly with Tes. The crystal structure of the 1-65(Arp7A)·LIM2-3(Tes)·EVH1(Mena) complex reveals that residues 28-49 of Arp7A contact the LIM2-3 domains of Tes. Two alanine residues from Arp7A that occupy equivalent apolar pockets in both LIM domains as well as an intervening GPAK linker that binds the LIM2-3 junction are critical for the Arp7A-Tes interaction. Equivalent occupied apolar pockets are also seen in the tandem LIM domain structures of LMO4 and Lhx3 bound to unrelated ligands. Our results indicate that apolar pocket interactions are a common feature of tandem LIM domain interactions, but ligand specificity is principally determined by the linker sequence.

Indexed as

AnimalsCytoskeletal ProteinsCytoskeletonHomeodomain ProteinsHumansLIM Domain ProteinsMaleMicrofilament ProteinsProtein BindingProtein Structure, TertiaryRatsRNA-Binding ProteinsTumor Suppressor ProteinsCytoskeletal ProteinsEnah protein, humanHomeodomain ProteinsLIM Domain ProteinsMicrofilament ProteinsRNA-Binding ProteinsTES protein, humanTumor Suppressor Proteins

Identifiers

PMID21278383
PMCPMC3064208
OpenAlexW1980762494

What OpenQuestion holds

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LicenceCC BY-NC
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.