• Record: found
  • Abstract: found
  • Article: not found

ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif.

European Journal of Cell Biology

Amino Acid Sequence, Animals, Base Sequence, Cell Compartmentation, physiology, Cell Line, Cloning, Molecular, DNA, Complementary, chemistry, Endoplasmic Reticulum, Genetic Code, Golgi Apparatus, Humans, Lysine, analysis, Mannose-Binding Lectins, Membrane Proteins, genetics, Molecular Sequence Data, Molecular Weight, Oligonucleotides, chemical synthesis

Read this article at

      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


      Overlapping cDNAs encoding the entire human ERGIC-53, a 53 kDa membrane protein of the ER-Golgi intermediate compartment, have been isolated and their nucleotide sequence determined. The isolated cDNA is about 2.7 kb in length. The deduced polypeptide chain for ERGIC-53 consists of 510 amino acids (M(r) 54217) including an N-terminal signal sequence of 30 amino acids, a single putative transmembrane segment of 18 amino acids, and a short cytoplasmic domain of 12 amino acids. Surprisingly, the cytoplasmic segment contains two lysines positioned three and four residues from the C-terminus. Such a double lysine motif is known to function as a retention signal for a group of membrane proteins associated with the ER. Expression of a full-length cDNA of ERGIC-53 in Vero cells revealed intracellular localization similar but not always identical to the endogenously expressed ERGIC-53. The presence of an ER retention motif in a protein of the ER-Golgi intermediate compartment has important implications for the retention mechanism mediated by this signal.

      Related collections

      Author and article information



      Comment on this article