PIM 3 kinase, a proto-oncogene product, regulates phosphorylation of the measles virus nucleoprotein tail domain at Ser 479 and Ser 510.
Biochem Biophys Res Commun
; 531(3): 267-274, 2020 10 20.
Article
en En
| MEDLINE
| ID: mdl-32800554
ABSTRACT
The tail domain of the measles virus (MeV) N protein is typically phosphorylated at S479 and S510. However, the protein kinase responsible for this phosphorylation has not been identified. To identify the protein kinase responsible, we conducted an in vitro kinase assay in the presence of various protein kinase inhibitors. Phosphorylation of S479 and S510 was suppressed in the presence of SP600125. We demonstrated that purified PIM 3 kinase, which is sensitive to SP600125, successfully phosphorylated both phosphorylation sites. Inhibitors of PIM kinase, CX6258 and LY294002, also suppressed phosphorylation of the N protein. These findings indicate that PIM 3 kinase is associated with the tail domain of the N protein and that PIM 3 kinase regulates N protein phosphorylation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfoserina
/
Proteínas Proto-Oncogénicas
/
Proteínas Serina-Treonina Quinasas
/
Virus del Sarampión
/
Nucleoproteínas
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2020
Tipo del documento:
Article
País de afiliación:
Japón