A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail

Abstract The Target of Rapamycin Complex 1 (TORC1) involved in coordination of cell growth and metabolism is highly conserved among eukaryotes. Yet the signals and mechanisms controlling its activity differ among taxa, according to their biological specificities. A common feature of fungal and plant...

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Autores principales:	Elie Saliba, Cecilia Primo, Nadia Guarini, Bruno André
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/23ee4cea68474887b7ecd05b480743c3
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spelling	oai:doaj.org-article:23ee4cea68474887b7ecd05b480743c32021-12-02T13:33:51ZA plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail10.1038/s41598-021-83525-12045-2322https://doaj.org/article/23ee4cea68474887b7ecd05b480743c32021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83525-1https://doaj.org/toc/2045-2322Abstract The Target of Rapamycin Complex 1 (TORC1) involved in coordination of cell growth and metabolism is highly conserved among eukaryotes. Yet the signals and mechanisms controlling its activity differ among taxa, according to their biological specificities. A common feature of fungal and plant cells, distinguishing them from animal cells, is that their plasma membrane contains a highly abundant H+-ATPase which establishes an electrochemical H+ gradient driving active nutrient transport. We have previously reported that in yeast, nutrient-uptake-coupled H+ influx elicits transient TORC1 activation and that the plasma-membrane H+-ATPase Pma1 plays an important role in this activation, involving more than just establishment of the H+ gradient. We show here that the PMA2 H+-ATPase from the plant Nicotiana plumbaginifolia can substitute for Pma1 in yeast, to promote H+-elicited TORC1 activation. This H+-ATPase is highly similar to Pma1 but has a longer carboxy-terminal tail binding 14–3–3 proteins. We report that a C-terminally truncated PMA2, which remains fully active, fails to promote H+-elicited TORC1 activation. Activation is also impaired when binding of PMA2 to 14–3–3 s is hindered. Our results show that at least some plant plasma-membrane H+-ATPases share with yeast Pma1 the ability to promote TORC1 activation in yeast upon H+-coupled nutrient uptake.Elie SalibaCecilia PrimoNadia GuariniBruno AndréNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Elie Saliba Cecilia Primo Nadia Guarini Bruno André A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
description	Abstract The Target of Rapamycin Complex 1 (TORC1) involved in coordination of cell growth and metabolism is highly conserved among eukaryotes. Yet the signals and mechanisms controlling its activity differ among taxa, according to their biological specificities. A common feature of fungal and plant cells, distinguishing them from animal cells, is that their plasma membrane contains a highly abundant H+-ATPase which establishes an electrochemical H+ gradient driving active nutrient transport. We have previously reported that in yeast, nutrient-uptake-coupled H+ influx elicits transient TORC1 activation and that the plasma-membrane H+-ATPase Pma1 plays an important role in this activation, involving more than just establishment of the H+ gradient. We show here that the PMA2 H+-ATPase from the plant Nicotiana plumbaginifolia can substitute for Pma1 in yeast, to promote H+-elicited TORC1 activation. This H+-ATPase is highly similar to Pma1 but has a longer carboxy-terminal tail binding 14–3–3 proteins. We report that a C-terminally truncated PMA2, which remains fully active, fails to promote H+-elicited TORC1 activation. Activation is also impaired when binding of PMA2 to 14–3–3 s is hindered. Our results show that at least some plant plasma-membrane H+-ATPases share with yeast Pma1 the ability to promote TORC1 activation in yeast upon H+-coupled nutrient uptake.
format	article
author	Elie Saliba Cecilia Primo Nadia Guarini Bruno André
author_facet	Elie Saliba Cecilia Primo Nadia Guarini Bruno André
author_sort	Elie Saliba
title	A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
title_short	A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
title_full	A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
title_fullStr	A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
title_full_unstemmed	A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail
title_sort	plant plasma-membrane h+-atpase promotes yeast torc1 activation via its carboxy-terminal tail
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/23ee4cea68474887b7ecd05b480743c3
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A plant plasma-membrane H+-ATPase promotes yeast TORC1 activation via its carboxy-terminal tail

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