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The Identification of FERONIA‑interacting proteins in Arabidopsis thaliana via mass spectrometry

ABSTRACT: FERONIA (FER) is a plasma membrane-localized receptor-like kinase (RLK) that belongs to the Catharantus roseus RLK1-like (CrRLK1L) subfamily. FER serves as a potential cell wall sensor that regulates multiple phytohormones, including ABA, JA, SA, BR, auxin, and ethyl, but the underlying regulatory mechanisms are still largely unknown. To further understand how FER regulates downstream signaling pathway, we performed FER-interacting proteins via immunoprecipitation-mass spectrometry (IP-MS) assay generated from FER-GFP transgenic plants.

INSTRUMENT(S): Q Exactive HF-X

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

TISSUE(S): Plant Cell, Shoot

SUBMITTER: Chunzhao Zhao

LAB HEAD: Chunzhao Zhao

PROVIDER: PXD047596 | Pride | 2024-09-14

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20210318_HFX_ZCZ_LX_1209-S.msf	Msf
	20210318_HFX_ZCZ_LX_1209-S.raw	Raw
	20210318_HFX_ZCZ_LX_FER-S.msf	Msf
	20210318_HFX_ZCZ_LX_FER-S.raw	Raw
	20210318_HFX_ZCZ_LX_GFP-S.msf	Msf

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Similar Datasets

The interaction proteins of FER were identified by mass spectrometry

Project description:Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) family proteins are considered as potential cell wall sensors in plants. CrRLK1L subfamily proteins harbor two extracellular malectin-like domains that may bind to cell wall polymers, and an intracellular kinase domain that transmits signals via the phosphorylation of intracellular substrates. In Arabidopsis, there are 17 CrRLK1L family members, among which FER is the most widely studied. A growing body of evidence support that FER not only regulates plant growth and development, such as root hair development, pavement cell morphogenesis, flowering, and fertilization, but also controls plant responses to biotic and abiotic stresses. To decipher molecular mechanisms underlying the FER-mediated regulation of plant growth and development, we performed an immunoprecipitation-mass spectrometry (IP-MS) assay using FER-GFP transgenic plants to search for FER-interacting proteins.

2024-08-30 | PXD047595 | Pride

FERONIA controls ABA-mediated seed germination via the regulation of the kinase activity of CARK1

Project description:Seed germination is the initial step of the whole life cycle for an individual plant, and thus it needs to be tightly controlled to avoid the growth of plants under unfavorable conditions, such as high salinity and drought stress. It has been well known that ABA signaling pathway plays a key role in the regulation of seed germination. In this study, we found that FER, a receptor-like kinase that belongs to CrRLK1L subfamily, regulates seed germination under ABA or stress conditions via the modulation of ABI5 protein stability. Biochemical data indicate that FER interacts with and phosphorylates CARK1 protein, a receptor-like cytoplasmic kinase (RLCK) that is classified into the RLCK VIII subfamily. FER phosphorylates the Ser233 and Thr234 residues of CARK1, and these two residues are located in the activation loop and are required for the activation of CARK1. The CARK1 protein with the substitutions of these two amino acids to Ala exhibits reduced kinase activity and is not able to rescue the faster seed germination phenotype of cark1 mutant under ABA conditions. In both fer-4 and cark1 mutant, the ABA-triggered activation of SnRK2.6 and ABI5 protein accumulation were attenuated compared with the wild-type. Taken together, our study not only reveals a RLCK protein that functions directly downstream of FER to transduce external signals, but also provides a novel mechanistic insight into the understanding of seed germination regulation via ABA-mediated signaling pathways.

2024-09-14 | PXD047594 | Pride

FERONIA-mediated CC1 phosphorylation dynamically regulates cortical microtubule behavior and salt stress responses in Arabidopsis

Project description:Cell wall remodeling is important for plants to adapt to environmental stress, and therefore needs to be efficiently modulated during stress conditions. Under salt stress, cortical microtubules undergo a depolymerization-reassembly process to promote the biosynthesis of stress-adaptive cellulose, but the regulatory mechanisms underlying this process are still largely unknown. In this study, we reveal that FERONIA, a potential cell wall sensor, interacts with CC1 and its closest homolog, CC2; two proteins that are required for cortical microtubule reassembly under salt stress. Biochemical data indicate that FER phosphorylates CC1 on multiple residues in the second and third hydrophobic microtubule-binding regions in vitro and in vivo, and that these phosphorylations impact the ability of CC1 to engage with microtubules. Furthermore, FER kinase activity and the CC1 phosphorylation level were temporally coordinated upon exposure to salt stress, which coincided with dynamic microtubule reorganization. Both fer-4 and cc1 cc2 mutants displayed similar salt-sensitive phenotypes, which were related to compromised microtubule reassembly, corroborating that FER and CC1/CC2 function in the same pathway to regulate microtubule organization. Taken together, our study outlines an important intracellular mechanism that maintains microtubule dynamics during salt exposure in plant cells.

2024-08-30 | PXD047608 | Pride

Transcriptomic profile of FERONIA mutant treated with Aradopside

Project description:FERONIA (FER) receptor kinase has a versatile role in plant growth and development, biotic and abiotic stress responses, and reproduction. To gain new insights into the molecular interplay of these processes and to identify new functions of FER, we carried out quantitative transcriptome, proteome, and phosphoproteome profiling of wild type (WT) and a loss-of-function fer mutant in Arabidopsis plants. Gene Ontology terms for hormone signaling, abiotic stress, and biotic stress were significantly enriched among mis-expressed transcripts, proteins, and/or mis-phosphorylated proteins, in agreement with FER’s known roles in these processes. Analysis of multi-omics data and subsequent experimental evidence identified previously unknown functions of FER in ER (Endoplasmic Reticulum) body formation, glucosinolate biosynthesis. FER functions through transcription factor NAI1 to mediate ER body. FER also negatively regulates indole glucosinolates biosynthesis, partially through NAI1. Furthermore, we found that a group of abscisic acid (ABA)-induced transcription factors are hypo-phosphorylated in the fer mutant and demonstrated that FER acts through ABI5 to negatively regulate the ABA response during germination. Our integrated-omics study therefore reveals novel functions of FER and provides new insights into the underlying mechanisms of FER function.

2022-04-04 | GSE191303 | GEO

Transcriptomic profile of the FERONIA mutant

Project description:The goal of this study was to determine transcriptional changes in the FERONIA mutant (fer) in Arabidopsis leaves

2022-04-04 | GSE143634 | GEO

Transcriptome analysis of gene expression changes in fer-8 and the parental line

Project description:To reveal transcriptional changes in the fer-8 mutant that could explain the increase in Pseudomonas colonization, we performed transcriptional profiling in both shoots and roots from fer-8 and the parental line. We identified 675 up-regulated genes in the shoots of fer-8 relative to wildtype plants. Surprisingly, we found only 82 up-regulated genes in fer-8 roots relative to the parental line, and there were no significantly enriched GO terms. In contrast, we found that the genes upregulated in shoots were enriched in GO terms related to defense, response to fungi, and JA signaling, consistent with previous reports of JA activation in the shoots of another fer mutant fer-4.

2021-04-21 | GSE167143 | GEO

FERONIA regulates plant growth and survival under salt stress by modulating the dark reversion of phyB via a signature of phosphorylation

Project description:Here we report that FERONIA (FER) integrates phyB-mediated light signaling pathway to control salt stress response. Mutation in phytochrome B (phyB) largely suppresses the dwarfism and leaf bleaching phenotype of fer-4 mutant under salt stress. FER interacts with and phosphorylates the N-terminal domain of phyB. Mutation in fer-4 or disruption of the FER-mediated phosphorylation sites of phyB at Ser106 and Ser227 leads to a retention of phyB in the photobodies under dark conditions, suggesting that FER-mediated phosphorylation accelerates the dark reversion of phyB. Interestingly, salt stress slows down the dark reversion of phyB via the inhibition of the kinase activity of FER, and mutation of phyB or overexpression of PIF5 attenuates the salt-induced growth inhibition. Together, our study indicates that the plasma membrane-localized FER determines the dark reversion rate of phyB in the nucleus via a signature of phosphorylation and thus coordinates the extracellular stress signals and nuclear outputs to dynamically control plant growth and survival under stress conditions.

2021-11-08 | GSE188335 | GEO

Transcriptome analysis of differentially expressed genes in the feronia (fer-4) mutant

Project description:FERONIA (FER) receptor kinase is a multifunctional regulator controlling myriad plant growth and developmental processes and interactions with the environment. We perform a RNA-seq analysis of genes differentially expressed in fer-4 mutant and observed significant changes of groups of genes previously characterized to be involved in AUXIN, ABA, ethylene and RALF1 signaling. The Results provide insight into the molecular mechanisms of FERONIA participation in regulating peptide and hormone signaling.

2020-06-30 | GSE125468 | GEO

A regulatory module controls plant growth and stress response by modulating hormone level

Project description:Perception and relay of cell wall signals is critical for plants to regulate growth and stress responses, but the mechanism underlying this biological process remains largely unknown. Here we report that RAPID ALKALINIZATION FACTOR (RALFs) peptides, Leucine-rich repeat extensins (LRXs) and FERONIA (FER) are physically associated in extracellular region. lrx345, fer-4, and transgenic plants overexpressing RALF22 or RALF23 all showed retarded growth, increased sensitivity to salt stress, and constitutively increased levels of ABA, JA, and SA. Salt treatment or chemical disruption of cell wall promotes the release of mature RALF peptides, which negatively regulate the function of FER by inducing its internalization. JA mutants coi1 and aos restore the retarded growth, and mutation of ABA2 suppresses the salt-sensitive phenotype of lrx345. Together, we propose that LRXs, RALFs, and FER function as a module to sense and transduce cell wall signals, thereby regulating growth and stress responses via hormones-mediated pathways.

2021-07-15 | GSE114682 | GEO

Profiling FERONIA interaction proteins by Pupylation-based interacting tagging in Arabidopsis

Project description:FERONIA (FER) is a ubiquitious expressed and a plasma memberane-localized receptor-like protein kinase which modulate many biological functions. Elucidating the interacting proteins is the crucial step in understanding the molecular function of FER in regulating plant development. However, weak and transient interactions make identifying FER interacting proteins a challenge. Here, we adapted a novel proximity-based labelling technique, pupylation-based interaction tagging (PUP-IT), to label interacting proteins, subsequent enriched by affinity capture, and analyzed by liquid chromatography-coupled tandem mass spectrometery (LC-MS/MS) to profile FER interacting proteins. To perform a quick screen, a transient protoplasts expression system was conducted to identify interacting proteins in mesophyll cells. In addition, we generated a transgenic line that harboring a tagging substrate-inducible system and FER-ligase recombinant protein driven by a native promoter for surveying the interacting proteins in seedlings and flower organ. We introduce and prove the concept of PUP-IT tool designed to detect protein interactions of significance in plants.

2024-08-13 | PXD045546 | Pride

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