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PIM 3 kinase, a proto-oncogene product, regulates phosphorylation of the measles virus nucleoprotein tail domain at Ser 479 and Ser 510.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2020 Oct 20; Vol. 531 (3), pp. 267-274. Date of Electronic Publication: 2020 Aug 14. - Publication Year :
- 2020
-
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.<br />Competing Interests: Declaration of competing interest The authors declare no conflicts of interest.<br /> (Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Animals
Anthracenes pharmacology
Cell Line
Humans
Nucleocapsid Proteins
Phosphorylation drug effects
Protein Domains
Proto-Oncogene Mas
Measles virus metabolism
Nucleoproteins chemistry
Nucleoproteins metabolism
Phosphoserine metabolism
Protein Serine-Threonine Kinases metabolism
Proto-Oncogene Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 531
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 32800554
- Full Text :
- https://doi.org/10.1016/j.bbrc.2020.06.002