Post-translational modifications of histone proteins by monoamine neurotransmitters.
Journal
Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312
Informations de publication
Date de publication:
06 2023
06 2023
Historique:
received:
22
12
2022
revised:
13
03
2023
accepted:
14
03
2023
pmc-release:
01
06
2024
medline:
30
5
2023
pubmed:
14
4
2023
entrez:
13
4
2023
Statut:
ppublish
Résumé
Protein monoaminylation is a biochemical process through which biogenic monoamines (e.g., serotonin, dopamine, histamine, etc.) are covalently bonded to certain protein substrates via Transglutaminase 2, an enzyme that catalyzes the transamidation of primary amines to the γ-carboxamides of glutamine residues. Since their initial discovery, these unusual post-translational modifications have been implicated in a wide variety of biological processes, ranging from protein coagulation to platelet activation and G-protein signaling. More recently, histone proteins - specifically histone H3 at glutamine 5 (H3Q5) - have been added to the growing list of monoaminyl substrates in vivo, with H3Q5 monoaminylation demonstrated to regulate permissive gene expression in cells. Such phenomena have further been shown to contribute critically to various aspects of (mal)adaptive neuronal plasticity and behavior. In this short review, we examine the evolution of our understanding of protein monoaminylation events, highlighting recent advances in the elucidation of their roles as important chromatin regulators.
Identifiants
pubmed: 37054563
pii: S1367-5931(23)00040-6
doi: 10.1016/j.cbpa.2023.102302
pmc: PMC10225327
mid: NIHMS1885996
pii:
doi:
Substances chimiques
Histones
0
Glutamine
0RH81L854J
Biogenic Monoamines
0
Neurotransmitter Agents
0
Types de publication
Journal Article
Review
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
102302Subventions
Organisme : NIDA NIH HHS
ID : DP1 DA042078
Pays : United States
Organisme : NIDA NIH HHS
ID : R01 DA056595
Pays : United States
Organisme : NIMH NIH HHS
ID : R01 MH116900
Pays : United States
Informations de copyright
Copyright © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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