Actin R256 Mono-methylation Is a Conserved Post-translational Modification Involved in Transcription.
INO80
PRMT5
TAAD
actin
actin PTMs
arginine monomethylation
nuclear actin
transcription
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
29 09 2020
29 09 2020
Historique:
received:
16
09
2019
revised:
11
07
2020
accepted:
27
08
2020
entrez:
30
9
2020
pubmed:
1
10
2020
medline:
16
9
2021
Statut:
ppublish
Résumé
Nuclear actin has been elusive due to the lack of knowledge about molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on an evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions and cause diseases in human. Interestingly, we show that an antibody specific for actin R256me1 preferentially stains nuclear actin over cytoplasmic actin in yeast, mouse, and human cells. We also show that actin R256me1 is regulated by protein arginine methyl transferase-5 (PRMT5) in HEK293 cells. A genome-wide survey of actin R256me1 mark provides a landscape for nuclear actin correlated with transcription. Further, gene expression and protein interaction studies uncover extensive correlations between actin R256me1 and active transcription. The discovery of actin R256me1 mark suggests a fundamental mechanism to distinguish nuclear actin from cytoplasmic actin through post-translational modification (PTM) and potentially implicates an actin PTM mark in transcription and human diseases.
Identifiants
pubmed: 32997990
pii: S2211-1247(20)31161-X
doi: 10.1016/j.celrep.2020.108172
pmc: PMC8860185
mid: NIHMS1775293
pii:
doi:
Substances chimiques
Actins
0
Transcription Factors
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108172Subventions
Organisme : NCI NIH HHS
ID : K22 CA100017
Pays : United States
Organisme : NHLBI NIH HHS
ID : P01 HL110869
Pays : United States
Organisme : NIEHS NIH HHS
ID : R01 ES013768
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM093104
Pays : United States
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests B.F.P. has a financial interest in Piconic, LLC, which uses the ChIP-exo technology implemented in this study, and could potentially benefit from the outcomes of this research.
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