title: A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1.
abstract: Brefeldin A (BFA) is a unique drug affecting the molecular mechanisms that regulate membrane traffic and organelle structure. BFA's ability to alter retrograde traffic from the Golgi to the endoplasmic reticulum (ER) led us to ask whether the ERD-2 retrieval receptor, proposed to return escaped ER resident proteins from the Golgi, might either interfere with or mimic the effects of the drug. When either human ERD-2 or a novel human homolog (referred to as ELP-1) is overexpressed in a variety of cell types, the effects are phenotypically indistinguishable from the addition of BFA. These include the redistribution of the Golgi coat protein, beta-COP, to the cytosol, the loss of the Golgi apparatus as a distinct organelle, the mixing of this organelle with the ER, the addition of complex oligosaccharides to resident ER glycoproteins, and the block of anterograde traffic. Thus, these receptors may provide signals that regulate retrograde traffic between the Golgi and the ER.
authors.affiliation: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
authors.forename: V W
authors.initials: VW
authors.lastname: Hsu
authors.forename: N
authors.initials: N
authors.lastname: Shah
authors.forename: R D
authors.initials: RD
authors.lastname: Klausner
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D020126:Brefeldin A; D002352:Carrier Proteins; D002451:Cell Compartmentation / Q000187:drug effects*; D003001:Cloning, Molecular; D003517:Cyclopentanes / Q000494:pharmacology*; D004705:Endocytosis; D019204:GTP-Binding Proteins / Q000502:physiology; D015870:Gene Expression; D006056:Golgi Apparatus / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010641:Phenotype; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000502:physiology*; D016415:Sequence Alignment; D012995:Solubility; D014162:Transfection; D033921:Vesicular Transport Proteins
chemical_list: D002352:Carrier Proteins; D003517:Cyclopentanes; D008565:Membrane Proteins; D009838:Oligodeoxyribonucleotides; D011506:Proteins; D011956:Receptors, Cell Surface; D033921:Vesicular Transport Proteins; C074642:KDELR2 protein, human; D020126:Brefeldin A; D019204:GTP-Binding Proteins