Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs

• DOI: 10.1126/science.8128252
• Publication Date: 2006-10-06T00:01:25Z
• Authors: Pierre Cosson; François Letourneur
• Keywords: 0301 basic medicine; Lysine; Recombinant Fusion Proteins; Molecular Sequence Data; Golgi Apparatus; Membrane Proteins; Biological Transport; Endoplasmic Reticulum; Coatomer Protein; Cell Line; Fungal Proteins; 03 medical and health sciences; Hexosyltransferases; Transferases; Mutation; [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology; Animals; Amino Acid Sequence

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.