A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum

Cell. 1987 Jul 17;50(2):311-7. doi: 10.1016/0092-8674(87)90226-1.

Abstract

The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.

Publication types

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

MeSH terms

  • Adenovirus Early Proteins
  • Adenoviruses, Human / genetics
  • Antigens, Viral, Tumor / analysis
  • Endoplasmic Reticulum / analysis
  • Endoplasmic Reticulum / ultrastructure*
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • HeLa Cells / cytology
  • Humans
  • Mutation
  • Oncogene Proteins, Viral / analysis
  • Oncogene Proteins, Viral / genetics*
  • Oncogene Proteins, Viral / metabolism

Substances

  • Adenovirus Early Proteins
  • Antigens, Viral, Tumor
  • Oncogene Proteins, Viral