Rer1p, a Retrieval Receptor for Endoplasmic Reticulum Membrane Proteins, Is Dynamically Localized to the Golgi Apparatus by Coatomer

• Published in: The Journal of cell biology Vol. 152; no. 5; pp. 935 - 944
• Main Authors: Sato, Ken, Sato, Miyuki, Nakano, Akihiko
• Format: Journal Article
• Language: English
• Published: United States Rockefeller University Press 05.03.2001; The Rockefeller University Press
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Antibodies; binding proteins; cell membranes; Cells; chemistry; Coat Protein Complex I; Coat Protein Complex I - chemistry; Coat Protein Complex I - genetics; Coat Protein Complex I - metabolism; cytochemistry; cytology; Cytosol; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Fluorescence; Fungal Proteins; Fungal Proteins - chemistry; Fungal Proteins - genetics; Fungal Proteins - metabolism; genetics; Golgi apparatus; Golgi Apparatus - chemistry; Golgi Apparatus - metabolism; Guanine Nucleotide Exchange Factors; Intracellular Membranes; Intracellular Membranes - chemistry; Intracellular Membranes - metabolism; Lysine; Lysine - genetics; Lysine - metabolism; Membrane Glycoproteins; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; Membrane Proteins; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membranes; metabolism; Models, Biological; Molecular Sequence Data; Mutation; Original; Protein Binding; Protein Structure, Tertiary; Protein Subunits; Protein Transport; Proteins; Receptors; Recombinant Fusion Proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Recycling; Saccharomyces cerevisiae; Saccharomyces cerevisiae - cytology; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins; Sequence Alignment; Vacuoles; Vacuoles - metabolism; Vesicular Transport Proteins; Yeast; Yeasts
• ISSN: 0021-9525; 1540-8140; 1540-8140
• DOI: 10.1083/jcb.152.5.935

Rer1p, a yeast Golgi membrane protein, is required for the retrieval of a set of endoplasmic reticulum (ER) membrane proteins. We present the first evidence that Rer1p directly interacts with the transmembrane domain (TMD) of Sec12p which contains a retrieval signal. A green fluorescent protein (GFP) fusion of Rer1p rapidly cycles between the Golgi and the ER. Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole. The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing α and γ subunits. These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.