Inhibition of protein phosphorylation modulates expression of the Jak family protein tyrosine kinases

J Virol. 1995 Sep;69(9):5833-7. doi: 10.1128/JVI.69.9.5833-5837.1995.

Abstract

Treatment of murine Friend cells with a dose of the protein kinase inhibitor staurosporine, which is able to block the response of the cells to interferons, appears to inhibit phosphorylation of Jak proteins and, interestingly, to specifically reduce tyk2 and Jak1 expression and to increase Jak2 both in the presence and in the absence of interferons. Therefore, a potential role for phosphorylation events in the regulation of expression of the Jak family members is suggested.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaloids / pharmacology*
  • Animals
  • Friend murine leukemia virus / drug effects
  • Friend murine leukemia virus / physiology
  • Gene Expression* / drug effects
  • Interferon-alpha / pharmacology
  • Interferon-gamma / pharmacology
  • Janus Kinase 1
  • Janus Kinase 2
  • Leukemia, Experimental
  • Mice
  • Phosphorylation
  • Protein Biosynthesis*
  • Protein Kinase Inhibitors*
  • Protein-Tyrosine Kinases / biosynthesis*
  • Proto-Oncogene Proteins*
  • RNA, Messenger / analysis
  • RNA, Messenger / biosynthesis
  • Staurosporine
  • TYK2 Kinase
  • Tumor Cells, Cultured

Substances

  • Alkaloids
  • Interferon-alpha
  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins
  • RNA, Messenger
  • Interferon-gamma
  • Protein-Tyrosine Kinases
  • Jak1 protein, mouse
  • Jak2 protein, mouse
  • Janus Kinase 1
  • Janus Kinase 2
  • TYK2 Kinase
  • Tyk2 protein, mouse
  • Staurosporine