| Title: | "STE6, the yeast a-factor transporter" |
| Address: | "Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205" |
| ISSN/ISBN: | 1043-4682 (Print) 1043-4682 (Linking) |
| Abstract: | "In eukaryotic cells, most extracellular proteins exit the cell via the classical secretory pathway (ER-->Golgi-->secretory vesicles). A notable exception to this pattern is the Saccharomyces cerevisiae mating pheromone alpha-factor, an isoprenylated, methylated, oligopeptide signaling molecule which uses a distinctly non-classical mechanism for secretion. Export of alpha-factor from the yeast cell is mediated by STE6, a member of the ABC protein superfamily. STE6 is one of the few eukaryotic ABC proteins for which a true physiological substrate is known. The ability to carry out molecular manipulations with ease in yeast, together with the possibility of probing substrate-transporter interactions via genetic analysis, affords an excellent opportunity to rigorously dissect the workings of this ABC family member" |
| Keywords: | "ATP Binding Cassette Transporter, Subfamily B, Member 1 *ATP-Binding Cassette Transporters Amino Acid Sequence Biological Transport, Active Carrier Proteins/metabolism Drug Resistance Fungal Proteins/chemistry/*metabolism *Glycoproteins Membrane Glycoprot;" |
| Notes: | "MedlineMichaelis, S eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review England 1993/02/01 Semin Cell Biol. 1993 Feb; 4(1):17-27. doi: 10.1006/scel.1993.1003" |
