Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum

EMBO J. 1990 Oct;9(10):3153-62. doi: 10.1002/j.1460-2075.1990.tb07513.x.


Several families of transmembrane endoplasmic reticulum (ER) proteins contain retention motifs in their cytoplasmically exposed tails. Mutational analyses demonstrated that two lysines positioned three and four or five residues from the C-terminus represent the retention motif. The introduction of a lysine preceding the lysine that occurs three residues from the terminus of Lyt2 renders this cell surface protein a resident of the ER. Likewise, the appropriate positioning of two lysine residues in a poly-serine sequence confines marker proteins to the ER. Arginines or histidines cannot replace lysines, suggesting that simple charge interactions are not sufficient to explain the retention. The identified consensus motif may serve as a retrieval signal that brings proteins back from a sorting compartment adjacent to the ER.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD / genetics
  • Antigens, Differentiation, T-Lymphocyte / genetics
  • Base Sequence
  • CD8 Antigens
  • DNA, Recombinant / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • HeLa Cells / metabolism
  • Humans
  • Lysine
  • Membrane Proteins / analysis
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Mutation
  • Oligonucleotide Probes
  • Sequence Homology, Nucleic Acid


  • Antigens, CD
  • Antigens, Differentiation, T-Lymphocyte
  • CD8 Antigens
  • DNA, Recombinant
  • Membrane Proteins
  • Oligonucleotide Probes
  • Lysine