Evidence map›Paper›PMID 32738036›Full record

ReviewWiley interdisciplinary reviews. RNA2021

Molecular and biological functions of TRIM-NHL RNA-binding proteins.

Robert P Connacher, Aaron C Goldstrohm

Open access · greenAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

31 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. RNA-binding is the essential biological function of thebioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
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  9. Review
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  15. Review
  16. Multifaceted role ofMedComm · 2024
    Review
  17. Article
  18. Advances in the antitumor mechanisms of tripartite motif-containing protein 3.Journal of cancer research and clinical oncology · 2024
    Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Robert P ConnacherDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.ORCID 0000-0003-4560-3852
Aaron C GoldstrohmORCID 0000-0002-1867-8763
University of Minnesota · US

Funding

Request to Transfer R01GM105707-03 Novel regulatory mechanisms of Drosophila Pumilio and NanosR01GM105707 · NIGMS · UNIVERSITY OF MINNESOTA · PI GOLDSTROHM, AARON CHARLES · 2013 to 2022
$2.7M
mRNA regulatory functions of the Drosophila TRIM-NHL protein, BratR01GM145835 · NIGMS · UNIVERSITY OF MINNESOTA · PI GOLDSTROHM, AARON CHARLES · 2022 to 2025
$1.4M
NIGMS NIH HHS R01 GM105707NIGMS NIH HHS R01 GM145835
6 · The paper itself

Abstract

The TRIM-NHL family of proteins shares a conserved domain architecture and play crucial roles in stem cell biology, fertility, and development. This review synthesizes new insights that have revolutionized our understanding of the molecular and biological functions of TRIM-NHL proteins. Multiple TRIM-NHLs have been shown to bind specific RNA sequences and structures. X-ray crystal structures of TRIM-NHL proteins in complex with RNA ligands reveal versatile modes of RNA recognition by the NHL domain. Functional and genetic analyses show that TRIM-NHL RNA-binding proteins negatively regulate the protein expression from the target mRNAs that they bind. This repressive activity plays a crucial role in controlling stem cell fate in the developing brain and differentiating germline. To highlight these paradigms, we focus on several of the most-extensively studied TRIM-NHL proteins, specifically Drosophila and vertebrate TRIM71, among others. Brat is essential for development and regulates key target mRNAs to control differentiation of germline and neural stem cells. TRIM71 is also required for development and promotes stem cell proliferation while antagonizing differentiation. Moreover, TRIM71 can be utilized to help reprogram fibroblasts into induced pluripotent stem cells. Recently discovered mutations in TRIM71 cause the neurodevelopmental disease congenital hydrocephalus and emphasize the importance of its RNA-binding function in brain development. Further relevance of TRIM71 to disease pathogenesis comes from evidence linking it to several types of cancer, including liver and testicular cancer. Collectively, these advances demonstrate a primary role for TRIM-NHL proteins in the post-transcriptional regulation of gene expression in crucial biological processes. This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications Translation > Translation Regulation RNA Turnover and Surveillance > Regulation of RNA Stability.

Indexed as

RNA-Binding ProteinsUbiquitin-Protein LigasesAnimalsDNA-Binding ProteinsDrosophilaDrosophila ProteinsHumansMaleTripartite Motif Proteinsbrat protein, DrosophilaDNA-Binding ProteinsDrosophila ProteinsRNA-Binding ProteinsTRIM71 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligasesbrain developmentcancermRNA regulationneurological diseaseRNA decaysequence-specific RNA-binding proteinsstem cellstranslational controlTRIM NHL

Identifiers

PMID32738036
PMCPMC7855385
OpenAlexW3046404505

What OpenQuestion holds

Textmetadata
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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.