Regulation of human immunodeficiency virus Nef protein by phosphorylation

Virology. 1994 May 15;201(1):157-61. doi: 10.1006/viro.1994.1278.

Abstract

Human immunodeficiency virus isolates express a Nef protein with either an alanine or a threonine at amino acid residue 15. The threonine residue is a site for phosphorylation by protein kinase C. Jurkat T cells constitutively expressing the alanine variant of Nef exhibit the ability to downregulate the induction of transcription factors NF-kB and AP-1. In contrast, Jurkat cells with the threonine variant of Nef are at least partially restored in their ability to recruit NF-kB and AP-1.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • DNA, Viral / metabolism
  • Down-Regulation
  • Electrophoresis, Polyacrylamide Gel / methods
  • Gene Products, nef / analysis
  • Gene Products, nef / chemistry*
  • Gene Products, nef / physiology*
  • Genes, nef / genetics
  • HIV / chemistry
  • HIV / metabolism*
  • HIV Long Terminal Repeat / genetics
  • Humans
  • Interleukin-2 / genetics
  • NF-kappa B / biosynthesis*
  • Phosphorylation
  • Point Mutation
  • Promoter Regions, Genetic / genetics
  • Proto-Oncogene Proteins c-jun / biosynthesis*
  • Threonine / metabolism
  • Transcription, Genetic
  • Tumor Cells, Cultured
  • nef Gene Products, Human Immunodeficiency Virus

Substances

  • DNA, Viral
  • Gene Products, nef
  • Interleukin-2
  • NF-kappa B
  • Proto-Oncogene Proteins c-jun
  • nef Gene Products, Human Immunodeficiency Virus
  • Threonine