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.