| Title: | "Pep12p is a multifunctional yeast syntaxin that controls entry of biosynthetic, endocytic and retrograde traffic into the prevacuolar compartment" |
| Author(s): | Gerrard SR; Levi BP; Stevens TH; |
| Address: | "Institute of Molecular Biology, Department of Chemistry, University of Oregon, Eugene, OR 97403-1229, USA" |
| DOI: | 10.1034/j.1600-0854.2000.010308.x |
| ISSN/ISBN: | 1398-9219 (Print) 1398-9219 (Linking) |
| Abstract: | "Delivery of proteins to the vacuole of the yeast Saccharomyces cerevisiae requires the function of the endosomal syntaxin, Pep12p. Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we show that deletion of the carboxy-terminal transmembrane domain of Pep12p results in a temperature-conditional block in transport of CPY to the PVC. The PVC also receives traffic from the early endosome and the vacuole, and mutation in PEP12 also blocks these other trafficking pathways into the PVC. Therefore, Pep12p is a multifunctional syntaxin that is required for all known trafficking pathways into the yeast PVC. Finally, we found that the internalized pheromone receptor, Ste3p, can cycle out of the PVC in a VPS27-independent fashion" |
| Keywords: | "Endosomes/*metabolism Fungal Proteins/*physiology Membrane Fusion Membrane Proteins/metabolism/*physiology Models, Biological Organelles/metabolism Protein Transport/*physiology Qa-SNARE Proteins Receptors, Cell Surface/metabolism *Receptors, G-Protein-Co;" |
| Notes: | "MedlineGerrard, S R Levi, B P Stevens, T H eng GM32448/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 2001/02/24 Traffic. 2000 Mar; 1(3):259-69. doi: 10.1034/j.1600-0854.2000.010308.x" |
