Evidence map›Paper›PMID 36695883›Full record

ReviewCellular and molecular life sciences : CMLS2023

Type 2 transglutaminase in the nucleus: the new epigenetic face of a cytoplasmic enzyme.

Federica Rossin, Fabiola Ciccosanti, Manuela D'Eletto, Luca Occhigrossi, Gian Maria Fimia, Mauro Piacentini

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2023. 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
5.2field-weighted citation impact, top 4% 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, 20 citations in OpenAlex.

  1. Review
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  13. The Role of Transglutaminase 2 in Cancer: An Update.International journal of molecular sciences · 2024
    Review
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  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

6 authors at 3 institutions in 2 countries.

Federica RossinDepartment of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy.
Fabiola CiccosantiDepartment of Epidemiology, Preclinical Research and Advanced Diagnostics, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Rome, Italy.
Manuela D'ElettoDepartment of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy.
Luca OcchigrossiDepartment of Molecular Medicine, University of Rome "La Sapienza", Rome, Italy.
Gian Maria FimiaDepartment of Epidemiology, Preclinical Research and Advanced Diagnostics, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Rome, Italy.
Mauro PiacentiniDepartment of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy. mauro.piacentini@uniroma2.it.ORCID http://orcid.org/0000-0003-2919-1296
University of Rome Tor Vergata · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITSapienza University of Rome · IT

Funding

Associazione Italiana per la Ricerca sul Cancro IG2018-21880Associazione Italiana Ricerca Alzheimer Airalzh-AGYR2020Fondazione per la Ricerca sulla Fibrosi Cistica FFC#15/2020Fondazione per la Ricerca sulla Fibrosi Cistica FFC#4/2021Fondazione per la Ricerca sulla Fibrosi Cistica FFC#8/2022
6 · The paper itself

Abstract

One of the major mysteries in science is how it is possible to pack the cellular chromatin with a total length of over 1 m, into a small sphere with a diameter of 5 mm "the nucleus", and even more difficult to envisage how to make it functional. Although we know that compaction is achieved through the histones, however, the DNA needs to be accessible to the transcription machinery and this is allowed thanks to a variety of very complex epigenetic mechanisms. Either DNA (methylation) or post-translational modifications of histone proteins (acetylation, methylation, ubiquitination and sumoylation) play a crucial role in chromatin remodelling and consequently on gene expression. Recently the serotonylation and dopaminylation of the histone 3, catalyzed by the Transglutaminase type 2 (TG2), has been reported. These novel post-translational modifications catalyzed by a predominantly cytoplasmic enzyme opens a new avenue for future investigations on the enzyme function itself and for the possibility that other biological amines, substrate of TG2, can influence the genome regulation under peculiar cellular conditions. In this review we analyzed the nuclear TG2's biology by discussing both its post-translational modification of various transcription factors and the implications of its epigenetic new face. Finally, we will focus on the potential impact of these events in human diseases.

Indexed as

Chromatin Assembly and DisassemblyCytoplasmEpigenesis, GeneticHistonesTransglutaminasesAcetylationCell NucleusChromatinDNADNA MethylationHumansProtein Glutamine gamma Glutamyltransferase 2Protein Processing, Post-TranslationalChromatinDNAHistonesProtein Glutamine gamma Glutamyltransferase 2TGM2 protein, humanTransglutaminasescBAFEpigeneticInteractomeTG2Transcriptional factors

Identifiers

PMID36695883
PMCPMC9874183
OpenAlexW4317931278

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.