Two novel effectors of trafficking and maturation of the yeast plasma membrane H+-ATPase.

摘要: The endoplasmic reticulum (ER) is the entry site of proteins into endomembrane system. Proteins exit ER via coat protein II (COPII) vesicles in a selective manner, mediated either by direct interaction with COPII or aided cargo receptors. Despite fundamental role such receptors sorting, only few have been identified. To further define machinery that packages secretory and targets from to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized mediate trafficking maturation Pma1, essential yeast plasma membrane proton ATPase. Ydl121c (Exp1) an binds packaged vesicles, whose deletion causes retention Pma1. Ykl077w (Psg1) physically interacts Exp1 can be found I (COPI) but does not directly bind Loss Psg1 enhanced degradation Pma1 vacuole. Our findings suggest receptor aids affects its retrieval. More generally our work shows utility high content screens identification novel components.