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. 2020 Oct 20;531(3):267-274. doi: 10.1016/j.bbrc.2020.06.002. Epub 2020 Aug 14.

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.

Keywords: Measles virus; Nucleocapsid protein; PIM 3 kinase; Paramyxovirus; Phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anthracenes / pharmacology
  • Cell Line
  • Humans
  • Measles virus / metabolism*
  • Nucleocapsid Proteins
  • Nucleoproteins / chemistry*
  • Nucleoproteins / metabolism*
  • Phosphorylation / drug effects
  • Phosphoserine / metabolism*
  • Protein Domains
  • Protein Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins / metabolism*

Substances

  • Anthracenes
  • MAS1 protein, human
  • Nucleocapsid Proteins
  • Nucleoproteins
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins
  • nucleoprotein, Measles virus
  • Phosphoserine
  • pyrazolanthrone
  • PIM3 protein, human
  • Protein Serine-Threonine Kinases