The TORC1 effector kinase Npr1 fine tunes the inherent activity of the Mep2 ammonium transport protein.

Abstract:

:The TORC1 complex controls cell growth upon integrating nutritional signals including amino-acid availability. TORC1 notably adapts the plasma membrane protein content by regulating arrestin-mediated endocytosis of amino-acid transporters. Here we demonstrate that TORC1 further fine tunes the inherent activity of the ammonium transport protein, Mep2, a yeast homologue of mammalian Rhesus factors, independently of arrestin-mediated endocytosis. The TORC1 effector kinase Npr1 and the upstream TORC1 regulator Npr2 control Mep2 transport activity by phospho-silencing a carboxy-terminal autoinhibitory domain. Under poor nitrogen supply, Npr1 enables Mep2 S457 phosphorylation and thus ammonium transport activity. Supplementation of the preferred nitrogen source glutamine leads to Mep2 inactivation and instant S457 dephosphorylation via plasma membrane Psr1 and Psr2 redundant phosphatases. This study underscores that TORC1 also adjusts nutrient permeability to regulate cell growth in a fast and flexible response to environmental perturbation, establishing a hierarchy in the transporters to be degraded, inactivated or maintained active at the plasma membrane.

journal_name

Nat Commun

journal_title

Nature communications

authors

Boeckstaens M,Llinares E,Van Vooren P,Marini AM

doi

10.1038/ncomms4101

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

3101

issn

2041-1723

pii

ncomms4101

journal_volume

5

pub_type

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