Negative regulation of interferon-induced transmembrane protein 3 by SET7-mediated lysine monomethylation.
J Biol Chem
; 288(49): 35093-103, 2013 Dec 06.
Article
en En
| MEDLINE
| ID: mdl-24129573
ABSTRACT
Although lysine methylation is classically known to regulate histone function, its role in modulating antiviral restriction factor activity remains uncharacterized. Interferon-induced transmembrane protein 3 (IFITM3) was found monomethylated on its lysine 88 residue (IFITM3-K88me1) to reduce its antiviral activity, mediated by the lysine methyltransferase SET7. Vesicular stomatitis virus and influenza A virus infection increased IFITM3-K88me1 levels by promoting the interaction between IFITM3 and SET7, suggesting that this pathway could be hijacked to support infection; conversely, IFN-α reduced IFITM3-K88me1 levels. These findings may have important implications in the design of therapeutics targeting protein methylation against infectious diseases.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
N-Metiltransferasa de Histona-Lisina
/
Proteínas de Unión al ARN
/
Proteínas de la Membrana
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Biol Chem
Año:
2013
Tipo del documento:
Article