The yeast integral plasma membrane protein Ist2 belongs to a group of membrane proteins which are synthesized from localized mRNAs. The protein reaches the plasma membrane via the ER on a route operating independently of the classical secretory pathway. We have identified a complex peptide-sorting signal located at the extreme C-terminus. This sorting signal operates independently of targeting information in IST2 mRNA and sorting to the plasma membrane does not require She-mediated mRNA transport into daughter cells. Based on these results, we suggest a posttranslational mechanism, which leads to the concentration of Ist2 - via multimerization - at ER sites, followed by direct transport to the plasma membrane. This novel mechanism operates downstream of IST2 mRNA localization.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|