Independent transcriptomic and proteomic regulation by type I and II protein arginine methyltransferases.
cell biology
molecular biology
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
24 Sep 2021
24 Sep 2021
Historique:
received:
25
06
2020
revised:
21
06
2021
accepted:
09
08
2021
entrez:
10
9
2021
pubmed:
11
9
2021
medline:
11
9
2021
Statut:
epublish
Résumé
Protein arginine methyltransferases (PRMTs) catalyze the post-translational monomethylation (Rme1), asymmetric (Rme2a), or symmetric (Rme2s) dimethylation of arginine. To determine the cellular consequences of type I (Rme2a) and II (Rme2s) PRMTs, we developed and integrated multiple approaches. First, we determined total cellular dimethylarginine levels, revealing that Rme2s was ∼3% of total Rme2 and that this percentage was dependent upon cell type and PRMT inhibition status. Second, we quantitatively characterized
Identifiants
pubmed: 34505004
doi: 10.1016/j.isci.2021.102971
pii: S2589-0042(21)00939-1
pmc: PMC8417332
doi:
Types de publication
Journal Article
Langues
eng
Pagination
102971Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM037537
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM108646
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM126421
Pays : United States
Informations de copyright
© 2021 The Author(s).
Déclaration de conflit d'intérêts
M.T.B. is a co-founder of EpiCypher.
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