Fatty acid modification of the coxsackievirus and adenovirus receptor. Academic Article uri icon

Overview

MeSH

  • Acylation
  • Adenoviridae
  • Animals
  • Bronchi
  • CHO Cells
  • COS Cells
  • Cells, Cultured
  • Coxsackie and Adenovirus Receptor-Like Membrane Protein
  • Cricetinae
  • Epithelial Cells
  • Gene Expression Regulation
  • Genetic Vectors
  • Humans

MeSH Major

  • Palmitates
  • Receptors, Virus

abstract

  • Membrane-proximal cysteines 259 and 260 in the cytoplasmic tail of the coxsackievirus and adenovirus receptor (CAR) are known to be essential for the tumor suppression activity of CAR. We demonstrate that these residues provide an S-acylation motif for modification of CAR with the fatty acid palmitate. Substitution of alanine for cysteines 259 and 260 results in the additional localization of CAR in perinuclear compartments with no effect on the efficiency of adenovirus infection. The results indicate that palmitylation is important for stable plasma membrane expression and biological activity of CAR but is not critical for adenovirus receptor performance.

publication date

  • June 2002

has subject area

  • Acylation
  • Adenoviridae
  • Animals
  • Bronchi
  • CHO Cells
  • COS Cells
  • Cells, Cultured
  • Coxsackie and Adenovirus Receptor-Like Membrane Protein
  • Cricetinae
  • Epithelial Cells
  • Gene Expression Regulation
  • Genetic Vectors
  • Humans
  • Palmitates
  • Receptors, Virus

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC136239

PubMed ID

  • 12021372

Additional Document Info

start page

  • 6382

end page

  • 6386

volume

  • 76

number

  • 12