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

TY - JOUR

T1 - Two novel effectors of trafficking and maturation of the yeast plasma membrane H+ -ATPase

AU - Geva, Yosef

AU - Crissman, Jonathan

AU - Arakel, Eric C

AU - Gómez-Navarro, Natalia

AU - Chuartzman, Silvia G

AU - Stahmer, Kyle R

AU - Schwappach, Blanche

AU - Miller, Elizabeth A

AU - Schuldiner, Maya

N1 - © 2017 The Authors. Traffic published by John Wiley & Sons Ltd.

PY - 2017/10

Y1 - 2017/10

N2 - 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.

AB - 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.

KW - COP-Coated Vesicles/metabolism

KW - Golgi Apparatus/metabolism

KW - Protein Binding

KW - Protein Transport

KW - Proton-Translocating ATPases/genetics

KW - Saccharomyces cerevisiae/genetics

KW - Saccharomyces cerevisiae Proteins/genetics

KW - Vesicular Transport Proteins/genetics

U2 - 10.1111/tra.12503

DO - 10.1111/tra.12503

M3 - SCORING: Journal article

C2 - 28727280

VL - 18

SP - 672

EP - 682

JO - TRAFFIC

JF - TRAFFIC

SN - 1398-9219

IS - 10

ER -