| Title: | Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p |
| Author(s): | Foley DA; Sharpe HJ; Otte S; |
| Address: | "Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Illinois, USA" |
| DOI: | 10.1080/09687860601178518 |
| ISSN/ISBN: | 0968-7688 (Print) 0968-7688 (Linking) |
| Abstract: | "Secretory proteins are transported from the endoplasmic reticulum to the Golgi apparatus via COPII-coated intermediates. Yeast Erv29p is a transmembrane protein cycling between these compartments. It is conserved across species, with one ortholog found in each genome studied, including the surf-4 protein in mammals. Yeast Erv29p acts as a receptor, loading a specific subset of soluble cargo, including glycosylated alpha factor pheromone precursor and carboxypeptidase Y, into vesicles. As the eukaryotic secretory pathway is highly conserved, mammalian surf-4 may perform a similar role in the transport of unknown substrates. Here we report the membrane topology of yeast Erv29p, which we solved by minimally invasive cysteine accessibility scanning using thiol-specific biotinylation and fluorescent labeling methods. Erv29p contains four transmembrane domains with both termini exposed to the cytosol. Two luminal loops may contain a recognition site for hydrophobic export signals on soluble cargo" |
| Keywords: | "Animals Binding Sites Endoplasmic Reticulum/metabolism Golgi Apparatus/metabolism Intracellular Membranes/chemistry Membrane Proteins/*chemistry Molecular Probe Techniques Protein Structure, Tertiary Saccharomyces cerevisiae Proteins/*chemistry Vesicular;" |
| Notes: | "MedlineFoley, Deirdre A Sharpe, Hayley J Otte, Stefan eng England 2007/05/24 Mol Membr Biol. 2007 Jul-Aug; 24(4):259-68. doi: 10.1080/09687860601178518" |
