PT - JOURNAL ARTICLE AU - Cosson, P AU - Letourneur, F TI - Coatomer interaction with di-lysine endoplasmic reticulum retention motifs AID - 10.1126/science.8128252 DP - 1994 Mar 18 TA - Science PG - 1629--1631 VI - 263 IP - 5153 4099 - http://science.sciencemag.org/content/263/5153/1629.short 4100 - http://science.sciencemag.org/content/263/5153/1629.full SO - Science1994 Mar 18; 263 AB - Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals.