Evidence map›Paper›PMID 27303792›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Crystal structure of a dimerization domain of human Caprin-1: insights into the assembly of an evolutionarily conserved ribonucleoprotein complex consisting of Caprin-1, FMRP and G3BP1.

Yuhong Wu, Jiang Zhu, Xiaolan Huang, Zhihua Du

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. CAPRIN1Cellular and molecular life sciences : CMLS · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Role of caprin-1 in carcinogenesis.Oncology letters · 2019
    Review
  17. Article
  18. Article
  19. 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 2 institutions in 1 country.

Yuhong WuDepartment of Chemistry and Biochemistry, Southern Illinois University, 1245 Lincoln Drive, Carbondale, IL 62901, USA.
Jiang ZhuDepartment of Chemistry and Biochemistry, Southern Illinois University, 1245 Lincoln Drive, Carbondale, IL 62901, USA.
Xiaolan HuangDepartment of Computer Science, Southern Illinois University, 1000 Faner Drive, Carbondale, IL 62901, USA.
Zhihua DuDepartment of Chemistry and Biochemistry, Southern Illinois University, 1245 Lincoln Drive, Carbondale, IL 62901, USA.
Southern Illinois University Carbondale · USScienceSouth · US

Funding

Molecular determinants of Caprin1-partner protein interactionsR15GM116062 · NIGMS · SOUTHERN ILLINOIS UNIVERSITY CARBONDALE · PI DU, ZHIHUA · 2015 to 2015
$333k
NIGMS NIH HHS R15 GM116062
6 · The paper itself

Abstract

Caprin-1 plays roles in many important biological processes, including cellular proliferation, innate immune response, stress response and synaptic plasticity. Caprin-1 has been implicated in several human diseases, including osteosarcoma, breast cancer, viral infection, hearing loss and neurodegenerative disorders. The functions of Caprin-1 depend on its molecular-interaction network. Direct interactions have been established between Caprin-1 and the fragile X mental retardation protein (FMRP), Ras GAP-activating protein-binding protein 1 (G3BP1) and the Japanese encephalitis virus (JEV) core protein. Here, crystal structures of a fragment (residues 132-251) of Caprin-1, which adopts a novel all-α-helical fold and mediates homodimerization through a substantial interface, are reported. Homodimerization creates a large and highly negatively charged concave surface suggestive of a protein-binding groove. The FMRP-interacting sequence motif forms an integral α-helix in the dimeric Caprin-1 structure in such a way that the binding of FMRP would not disrupt the homodimerization of Caprin-1. Based on insights from the structures and existing biochemical data, the existence of an evolutionarily conserved ribonucleoprotein (RNP) complex consisting of Caprin-1, FMRP and G3BP1 is proposed. The JEV core protein may bind Caprin-1 at the negatively charged putative protein-binding groove and an adjacent E-rich sequence to hijack the RNP complex.

Indexed as

Amino Acid SequenceBinding SitesCarrier ProteinsCell Cycle ProteinsDNA HelicasesFragile X Messenger Ribonucleoprotein 1HumansModels, MolecularPoly-ADP-Ribose Binding ProteinsProtein BindingProtein DomainsProtein Interaction Domains and MotifsProtein MultimerizationRNA HelicasesRNA Recognition Motif ProteinsSequence AlignmentCAPRIN1 protein, humanCarrier ProteinsCell Cycle ProteinsDNA HelicasesFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1G3BP1 protein, humanPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsCaprin-1Caprin-2FMRPG3BP1JEV core proteinRNA stress granule

Identifiers

PMID27303792
PMCPMC4908866
OpenAlexW2394809049

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.