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Two novel effectors of trafficking and maturation of the yeast plasma membrane H + ‐ ATPase
Author(s) -
Geva Yosef,
Crissman Jonathan,
Arakel Eric C.,
GómezNavarro Natalia,
Chuartzman Silvia G.,
Stahmer Kyle R.,
Schwappach Blanche,
Miller Elizabeth A.,
Schuldiner Maya
Publication year - 2017
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12503
Subject(s) - copii , copi , golgi apparatus , endoplasmic reticulum , microbiology and biotechnology , biology , endomembrane system , secretory pathway , vacuole , vesicle , clathrin adaptor proteins , protein targeting , transport protein , vesicular transport proteins , membrane protein , clathrin , biochemistry , membrane , vacuolar protein sorting , cytoplasm
The endoplasmic reticulum ( ER ) is the entry site of proteins into the endomembrane system. Proteins exit the ER via coat protein II ( COPII ) vesicles in a selective manner, mediated either by direct interaction with the COPII coat or aided by cargo receptors. Despite the fundamental role of such receptors in protein sorting, only a few have been identified. To further define the machinery that packages secretory cargo and targets proteins from the ER to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized proteins that mediate the trafficking and maturation of Pma1, the essential yeast plasma membrane proton ATPase . Ydl121c (Exp1) is an ER protein that binds Pma1, is packaged into COPII vesicles, and whose deletion causes ER retention of Pma1. Ykl077w (Psg1) physically interacts with Exp1 and can be found in the Golgi and coat protein I ( COPI ) vesicles but does not directly bind Pma1. Loss of Psg1 causes enhanced degradation of Pma1 in the vacuole. Our findings suggest that Exp1 is a Pma1 cargo receptor and that Psg1 aids Pma1 maturation in the Golgi or affects its retrieval. More generally our work shows the utility of high content screens in the identification of novel trafficking components.