Evidence map›Paper›PMID 34091597›Full record

ArticleCell death & disease2021

The RNA-binding protein HuR is a novel target of Pirh2 E3 ubiquitin ligase.

Alexandra Daks, Alexey Petukhov, Olga Fedorova, Oleg Shuvalov, Alena Kizenko, Elizaveta Tananykina, Elena Vasileva, Oleg Semenov, Andrew Bottrill, Nickolai Barlev

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. CRL2BMC biology · 2025
    Article
  7. Review
  8. Review
  9. RCHY1 and OPTN are required for melanophagy, selective autophagy of melanosomes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. p53 Affects Zeb1 Interactome of Breast Cancer Stem Cells.International journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
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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

10 authors at 4 institutions in 2 countries.

Alexandra DaksInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation. alexandra.daks@gmail.com.ORCID 0000-0003-0495-1244
Alexey PetukhovInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.
Olga FedorovaInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.
Oleg ShuvalovInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.
Alena KizenkoInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.ORCID 0000-0002-3759-8363
Elizaveta TananykinaInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.
Elena VasilevaInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.ORCID 0000-0003-2026-1331
Oleg SemenovInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation.
Andrew BottrillSchool of Life Sciences, University of Warwick, Coventry, CV4 7AL, UK.ORCID 0000-0002-5182-3643
Nickolai BarlevInstitute of Cytology, Russian Academy of Sciences, 194064, St Petersburg, Russian Federation. nick.a.barlev@gmail.com.
Institute of Cytology · RUFederal Almazov North-West Medical Research Centre · RUMoscow Institute of Physics and Technology · RUUniversity of Warwick · GB

Funding

Russian Foundation for Basic Research (RFBR) 18-29-09144Russian Science Foundation (RSF) 18-75-10076
6 · The paper itself

Abstract

The RING-finger protein Pirh2 is a p53 family-specific E3 ubiquitin ligase. Pirh2 also ubiquitinates several other important cellular factors and is involved in carcinogenesis. However, its functional role in other cellular processes is poorly understood. To address this question, we performed a proteomic search for novel interacting partners of Pirh2. Using the GST-pulldown approach combined with LC-MS/MS, we revealed 225 proteins that interacted with Pirh2. We found that, according to the GO description, a large group of Pirh2-associated proteins belonged to the RNA metabolism group. Importantly, one of the identified proteins from that group was an RNA-binding protein ELAVL1 (HuR), which is involved in the regulation of splicing and protein stability of several oncogenic proteins. We demonstrated that Pirh2 ubiquitinated the HuR protein facilitating its proteasome-mediated degradation in cells. Importantly, the Pirh2-mediated degradation of HuR occurred in response to heat shock, thereby affecting the survival rate of HeLa cells under elevated temperature. Functionally, Pirh2-mediated degradation of HuR augmented the level of c-Myc expression, whose RNA level is otherwise attenuated by HuR. Taken together, our data indicate that HuR is a new target of Pirh2 and this functional interaction contributes to the heat-shock response of cancer cells affecting their survival.

Indexed as

Cell Line, TumorELAV-Like Protein 1HEK293 CellsHeLa CellsHumansOncogenesRNA-Binding ProteinsUbiquitin-Protein LigasesELAVL1 protein, humanELAV-Like Protein 1RCHY1 protein, humanRNA-Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID34091597
PMCPMC8179929
OpenAlexW3167326398

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.