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The yeast H +-ATPase Pma1 promotes Rag/Gtr-dependent TORC1 activation in response to H +-coupled nutrient uptake

The yeast H +-ATPase Pma1 promotes Rag/Gtr-dependent TORC1 activation in response to H +-coupled nutrient uptake

Elie Saliba, Minoas Evangelinos, Christos Gournas, Florent Corrillon, Isabelle Georis, Bruno André

Elife. 2018 Mar 23;7:e31981.

PMID: 29570051

Abstract:

The yeast Target of Rapamycin Complex 1 (TORC1) plays a central role in controlling growth. How amino acids and other nutrients stimulate its activity via the Rag/Gtr GTPases remains poorly understood. We here report that the signal triggering Rag/Gtr-dependent TORC1 activation upon amino-acid uptake is the coupled H+ influx catalyzed by amino-acid/H+ symporters. H+-dependent uptake of other nutrients, ionophore-mediated H+ diffusion, and inhibition of the vacuolar V-ATPase also activate TORC1. As the increase in cytosolic H+ elicited by these processes stimulates the compensating H+-export activity of the plasma membrane H+-ATPase (Pma1), we have examined whether this major ATP-consuming enzyme might be involved in TORC1 control. We find that when the endogenous Pma1 is replaced with a plant H+-ATPase, H+ influx or increase fails to activate TORC1. Our results show that H+ influx coupled to nutrient uptake stimulates TORC1 activity and that Pma1 is a key actor in this mechanism.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1000849911	Hydrogen ionophore V		1000849-91-1	Price

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