Evidence map›Paper›PMID 33495566›Full record

ArticleCommunications biology2021

PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling.

Mamta Verma, Mohd Imran K Khan, Rajashekar Varma Kadumuri, Baskar Chakrapani, Sharad Awasthi, Arun Mahesh, Gayathri Govindaraju, Pavithra L Chavali, Arumugam Rajavelu, Sreenivas Chavali and 1 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025
    Review
  6. Review
  7. The Significance of Aldehyde Dehydrogenase 1 in Cancers.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Frontiers in immunology · 2022
    Article
  14. Article
  15. 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

11 authors at 4 institutions in 1 country.

Mamta Verma *Department of Biotechnology, Pondicherry University, Puducherry, 605014, India.ORCID 0000-0002-0943-0264
Mohd Imran K Khan *Department of Biotechnology, Pondicherry University, Puducherry, 605014, India.
Rajashekar Varma KadumuriDepartment of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati, Andhra Pradesh, 517507, India.
Baskar ChakrapaniDepartment of Biotechnology, Pondicherry University, Puducherry, 605014, India.
Sharad AwasthiDepartment of Biotechnology, Pondicherry University, Puducherry, 605014, India.
Arun MaheshDepartment of Biotechnology, Pondicherry University, Puducherry, 605014, India.
Gayathri GovindarajuInterdisciplinary Biology, Rajiv Gandhi Centre for Biotechnology, Trivandrum, Kerala, 695014, India.
Pavithra L ChavaliCSIR-Centre for Cellular & Molecular Biology, Hyderabad, Telangana, 500007, India.
Arumugam RajaveluInterdisciplinary Biology, Rajiv Gandhi Centre for Biotechnology, Trivandrum, Kerala, 695014, India.
Sreenivas ChavaliDepartment of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati, Andhra Pradesh, 517507, India. schavali@iisertirupati.ac.in.ORCID 0000-0001-8307-1645
Arunkumar DhayalanDepartment of Biotechnology, Pondicherry University, Puducherry, 605014, India. arun.dbt@pondiuni.edu.in.ORCID 0000-0003-2588-9865
Pondicherry University · INIndian Institute of Science Education and Research, Tirupati · INRajiv Gandhi Centre for Biotechnology · INCentre for Cellular and Molecular Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 3 (PRMT3) regulates protein functions by introducing asymmetric dimethylation marks at the arginine residues in proteins. However, very little is known about the interaction partners of PRMT3 and their functional outcomes. Using yeast-two hybrid screening, we identified Retinal dehydrogenase 1 (ALDH1A1) as a potential interaction partner of PRMT3 and confirmed this interaction using different methods. ALDH1A1 regulates variety of cellular processes by catalyzing the conversion of retinaldehyde to retinoic acid. By molecular docking and site-directed mutagenesis, we identified the specific residues in the catalytic domain of PRMT3 that facilitate interaction with the C-terminal region of ALDH1A1. PRMT3 inhibits the enzymatic activity of ALDH1A1 and negatively regulates the expression of retinoic acid responsive genes in a methyltransferase activity independent manner. Our findings show that in addition to regulating protein functions by introducing methylation modifications, PRMT3 could also regulate global gene expression through protein-protein interactions.

Indexed as

Aldehyde Dehydrogenase 1 FamilyDown-RegulationGene Expression RegulationHEK293 CellsHumansProtein-Arginine N-MethyltransferasesProtein BindingRetinal DehydrogenaseSignal TransductionTretinoinAldehyde Dehydrogenase 1 FamilyALDH1A1 protein, humanPRMT3 protein, humanProtein-Arginine N-MethyltransferasesRetinal DehydrogenaseTretinoin

Identifiers

PMID33495566
PMCPMC7835222
OpenAlexW3125047599

What OpenQuestion 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 OpenQuestion graph.