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

Sci Rep. 2021 Feb 26;11(1):4788. doi: 10.1038/s41598-021-83525-1.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • Fungal Proteins / metabolism*
  • Mechanistic Target of Rapamycin Complex 1 / metabolism*
  • Nicotiana / metabolism*
  • Plant Proteins / metabolism*
  • Proton-Translocating ATPases / metabolism*
  • Yeasts / metabolism*

Substances

  • Fungal Proteins
  • Plant Proteins
  • Mechanistic Target of Rapamycin Complex 1
  • Proton-Translocating ATPases