Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs
- 18 March 1994
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 263 (5153) , 1629-1631
- https://doi.org/10.1126/science.8128252
Abstract
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.Keywords
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