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The interaction proteins of FER were identified by mass spectrometry

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive Plus

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

TISSUE(S): Plant Cell, Root, Shoot

SUBMITTER: Chunzhao Zhao

LAB HEAD: Chunzhao Zhao

PROVIDER: PXD047595 | Pride | 2024-08-30

REPOSITORIES: Pride

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

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2024-09-14 | PXD047596 | Pride

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2024-08-30 | PXD047608 | Pride

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2024-09-14 | PXD047594 | Pride

The LRX-RALF-FER cell wall integrity sensing module controls plant growth and salt stress responses by modulating multiple plant hormones

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2021-07-15 | GSE114682 | GEO

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2023-12-31 | GSE225299 | 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.

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