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


Journal

Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402

Informations de publication

Date de publication:
25 Jan 2023
Historique:
received: 10 10 2022
accepted: 10 01 2023
revised: 09 01 2023
entrez: 25 1 2023
pubmed: 26 1 2023
medline: 28 1 2023
Statut: epublish

Résumé

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.

Identifiants

pubmed: 36695883
doi: 10.1007/s00018-023-04698-8
pii: 10.1007/s00018-023-04698-8
pmc: PMC9874183
doi:

Substances chimiques

Chromatin 0
DNA 9007-49-2
Histones 0
Transglutaminases EC 2.3.2.13
TGM2 protein, human 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

52

Subventions

Organisme : Associazione Italiana per la Ricerca sul Cancro
ID : IG2018-21880
Organisme : Fondazione per la Ricerca sulla Fibrosi Cistica
ID : FFC#15/2020
Organisme : Fondazione per la Ricerca sulla Fibrosi Cistica
ID : FFC#8/2022
Organisme : Fondazione per la Ricerca sulla Fibrosi Cistica
ID : FFC#4/2021
Organisme : Associazione Italiana Ricerca Alzheimer
ID : Airalzh-AGYR2020

Informations de copyright

© 2023. The Author(s).

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Auteurs

Federica Rossin (F)

Department of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy.

Fabiola Ciccosanti (F)

Department of Epidemiology, Preclinical Research and Advanced Diagnostics, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Rome, Italy.

Manuela D'Eletto (M)

Department of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy.

Luca Occhigrossi (L)

Department of Molecular Medicine, University of Rome "La Sapienza", Rome, Italy.

Gian Maria Fimia (GM)

Department of Epidemiology, Preclinical Research and Advanced Diagnostics, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Rome, Italy.
Department of Molecular Medicine, University of Rome "La Sapienza", Rome, Italy.

Mauro Piacentini (M)

Department of Biology, University of Rome 'Tor Vergata', Via Della Ricerca Scientifica 1, 00133, Rome, Italy. mauro.piacentini@uniroma2.it.
Department of Epidemiology, Preclinical Research and Advanced Diagnostics, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Rome, Italy. mauro.piacentini@uniroma2.it.

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