RT Journal Article
SR Electronic
T1 Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
JF Science
JO Science
FD American Association for the Advancement of Science
SP 1629
OP 1631
DO 10.1126/science.8128252
VO 263
IS 5153
A1 Cosson, P
A1 Letourneur, F
YR 1994
UL http://science.sciencemag.org/content/263/5153/1629.abstract
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.