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Identification of flg22-responsive BSU1 phosphorylation sites

ABSTRACT: To investigate flg22-induced posttranslational modification of BSU1 family proteins, we performed metabolic Stable Isotope Labeling In Arabidopsis followed by Immuno-Precipitation and Mass Spectrometry (SILIA IP-MS) analysis, with the isotopes switched in replicate experiments.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Plant Cell, Shoot

SUBMITTER: Shouling Xu

LAB HEAD: Shouling Xu

PROVIDER: PXD016283 | Pride | 2023-03-10

REPOSITORIES: Pride

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			Action	DRS
	V20140825-07.raw	Raw
	V20140825-07_ITMSms2cid.pep.xml	Pepxml

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Publications

Deconvoluting signals downstream of growth and immune receptor kinases by phosphocodes of the BSU1 family phosphatases.

Park Chan Ho CH Bi Yang Y Youn Ji-Hyun JH Kim So-Hee SH Kim Jung-Gun JG Xu Nicole Y NY Shrestha Ruben R Burlingame Alma L AL Xu Shou-Ling SL Mudgett Mary Beth MB Kim Seong-Ki SK Kim Tae-Wuk TW Wang Zhi-Yong ZY

Nature plants 20220613 6

Hundreds of leucine-rich repeat receptor kinases (LRR-RKs) have evolved to control diverse processes of growth, development and immunity in plants, but the mechanisms that link LRR-RKs to distinct cellular responses are not understood. Here we show that two LRR-RKs, the brassinosteroid hormone receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1) and the flagellin receptor FLAGELLIN SENSING 2 (FLS2), regulate downstream glycogen synthase kinase 3 (GSK3) and mitogen-activated protein (MAP) kinases, respe ...[more]

PMID: 35697730

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SPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 2: EtHCD)

Project description:The recent discovery of SPY-catalyzed protein O-fucosylation reveals a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates important roles of SPY in diverse developmental and physiological processes, however, the upstream signal controlling SPY activity and the downstream substrate proteins O-fucosylated by SPY remain largely unknown. Here, we demonstrate that SPY mediates sugar-dependent growth. We further identify hundreds of O-fucosylated proteins using lectin affinity chromatography followed by mass spectrometry. All the O-fucosylation events quantified in proteomic analyses are undetectable or decreased in the spy mutants and thus likely catalyzed by SPY. The O-fucosylome includes mostly nuclear and cytosolic proteins. Many O-fucosylated proteins function in essential cellular processes, hormone signaling, and developmental programs, consistent with the genetic functions of SPY. The O-fucosylome also includes many proteins modified by O-linked-N-acetylglucosamine (O-GlcNAc) and by phosphorylation downstream of the target of rapamycin (TOR) kinase, revealing the convergence of these nutrient signaling pathways on key regulatory functions such as post-transcriptional/translational regulation and hormonal responses. Our study identifies numerous targets of SPY/O-fucosylation and potential nodes of crosstalk among sugar/nutrient signaling pathways, enabling future dissection of the signaling network that mediates sugar regulation of plant growth and development.

2023-05-10 | PXD038491 | Pride

SPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 1: HCD)

2023-05-10 | PXD038490 | Pride

Quantitative proteomic comparison between wild type Col and acinus-2 pinin-1 mutant using 15N metabolic labeling

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2022-02-04 | PXD030081 | Pride

15N Stable-isotope-labeling in Arabidopsis (SILIA) quantitative MS analysis of the AtACINUS interactome

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Quantitative proteomic comparison between wild type Col and sec-5 mutant using 15N metabolic labeling

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2023-05-10 | PXD017085 | Pride

Phylogenetic patterns in the microbial response to resource availability: amino acid incorporation in San Francisco Bay

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

Project description: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.

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