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A type 2C protein phosphatase activates high-affinity nitrate uptake by directly dephosphorylating NRT2.1 in Arabidopsis

ABSTRACT: Nitrate transporter NRT2.1, which plays a central role in high-affinity nitrate uptake in roots, is activated at the post-translational level in response to nitrogen (N) starvation. However, critical enzymes required for post-translational activation of NRT2.1 remain to be identified. Here, we show that a type 2C protein phosphatase, designated CEPD-induced phosphatase (CEPH), activates high-affinity nitrate uptake by directly dephosphorylating S501 of NRT2.1, a residue that functions as a negative phospho-switch. CEPH is predominantly expressed in epidermal and cortex cells in roots and up-regulated by N starvation via a CEPDL2/CEPD1/2-mediated long-distance signaling from shoots. Loss of CEPH leads to a marked decrease in high-affinity nitrate uptake, tissue nitrate content, and plant biomass. Collectively, our results identify CEPH as a crucial enzyme in N starvation-dependent activation of NRT2.1, providing molecular and mechanistic insights into how plants regulate high-affinity nitrate uptake at the post-translational level in response to the N environment.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Root

SUBMITTER: Yuri Ohkubo

LAB HEAD: Yoshikatsu Matsubayashi

PROVIDER: PXD022343 | Pride | 2021-03-02

REPOSITORIES: Pride

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			Action	DRS
	20191011_QE2_HTSPAL_ESI12cmRT_sand_AcOH_PE_2019-206_e4_1st_01.pep.xml	Pepxml
	20191011_QE2_HTSPAL_ESI12cmRT_sand_AcOH_PE_2019-206_e4_1st_01.prot.xml	Xml
	20191011_QE2_HTSPAL_ESI12cmRT_sand_AcOH_PE_2019-206_e4_1st_01.raw	Raw
	20191011_QE2_HTSPAL_ESI12cmRT_sand_AcOH_PE_2019-206_e4_1st_02.raw	Raw
	20191011_QE2_HTSPAL_ESI12cmRT_sand_AcOH_PE_2019-206_e4_2nd3rd_01.raw	Raw

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