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1.
Sci Adv ; 9(14): eadd4791, 2023 04 07.
Article in English | MEDLINE | ID: mdl-37027473

ABSTRACT

Cells maintain a constant dialog between the extracellular matrix and their plasma membrane to fine tune signal transduction processes. We found that the receptor kinase FERONIA (FER), which is a proposed cell wall sensor, modulates phosphatidylserine plasma membrane accumulation and nano-organization, a key regulator of Rho GTPase signaling in Arabidopsis. We demonstrate that FER is required for both Rho-of-Plant 6 (ROP6) nano-partitioning at the membrane and downstream production of reactive oxygen species upon hyperosmotic stimulus. Genetic and pharmacological rescue experiments indicate that phosphatidylserine is required for a subset of, but not all, FER functions. Furthermore, application of FER ligand shows that its signaling controls both phosphatidylserine membrane localization and nanodomains formation, which, in turn, tunes ROP6 signaling. Together, we propose that a cell wall-sensing pathway controls via the regulation of membrane phospholipid content, the nano-organization of the plasma membrane, which is an essential cell acclimation to environmental perturbations.


Subject(s)
Arabidopsis Proteins , Arabidopsis , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Phosphatidylserines/metabolism , Signal Transduction/physiology , Arabidopsis/metabolism , Phosphotransferases/genetics , Phosphotransferases/metabolism , Cell Membrane/metabolism , Plants/metabolism
2.
Development ; 148(14)2021 07 01.
Article in English | MEDLINE | ID: mdl-34137447

ABSTRACT

Arabidopsis VASCULATURE COMPLEXITY AND CONNECTIVITY (VCC) is a plant-specific transmembrane protein that controls the development of veins in cotyledons. Here, we show that the expression and localization of the auxin efflux carrier PIN-FORMED1 (PIN1) is altered in vcc developing cotyledons and that overexpression of PIN1-GFP partially rescues vascular defects of vcc in a dosage-dependent manner. Genetic analyses suggest that VCC and PINOID (PID), a kinase that regulates PIN1 polarity, are both required for PIN1-mediated control of vasculature development. VCC expression is upregulated by auxin, likely as part of a positive feedback loop for the progression of vascular development. VCC and PIN1 localized to the plasma membrane in pre-procambial cells but were actively redirected to vacuoles in procambial cells for degradation. In the vcc mutant, PIN1 failed to properly polarize in pre-procambial cells during the formation of basal strands, and instead, it was prematurely degraded in vacuoles. VCC plays a role in the localization and stability of PIN1, which is crucial for the transition of pre-procambial cells into procambial cells that are involved in the formation of basal lateral strands in embryonic cotyledons.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/embryology , Arabidopsis/genetics , Embryonic Development , Gene Expression Regulation, Plant , Arabidopsis Proteins/genetics , Biological Transport , Cotyledon/cytology , Cotyledon/genetics , Cotyledon/metabolism , Gene Expression Regulation, Developmental , Membrane Transport Proteins/genetics , Membrane Transport Proteins/metabolism , Mutation , Plant Leaves/genetics , Protein Serine-Threonine Kinases/genetics , Protein Serine-Threonine Kinases/metabolism
3.
Plant Cell ; 30(6): 1243-1257, 2018 06.
Article in English | MEDLINE | ID: mdl-29764985

ABSTRACT

Plants face temporal and spatial variation in nitrogen (N) availability. This includes heterogeneity in soil nitrate (NO3-) content. To overcome these constraints, plants modify their gene expression and physiological processes to optimize N acquisition. This plasticity relies on a complex long-distance root-shoot-root signaling network that remains poorly understood. We previously showed that cytokinin (CK) biosynthesis is required to trigger systemic N signaling. Here, we performed split-root experiments and used a combination of CK-related mutant analyses, hormone profiling, transcriptomic analysis, NO3- uptake assays, and root growth measurements to gain insight into systemic N signaling in Arabidopsis thaliana By comparing wild-type plants and mutants affected in CK biosynthesis and ABCG14-dependent root-to-shoot translocation of CK, we revealed an important role for active trans-zeatin (tZ) in systemic N signaling. Both rapid sentinel gene regulation and long-term functional acclimation to heterogeneous NO3- supply, including NO3- transport and root growth regulation, are likely mediated by the integration of tZ content in shoots. Furthermore, shoot transcriptome profiling revealed that glutamate/glutamine metabolism is likely a target of tZ root-to-shoot translocation, prompting an interesting hypothesis regarding shoot-to-root communication. Finally, this study highlights tZ-independent pathways regulating gene expression in shoots as well as NO3- uptake activity in response to total N deprivation.


Subject(s)
Arabidopsis/metabolism , Nitrogen/metabolism , Plant Shoots/metabolism , Zeatin/metabolism , Arabidopsis Proteins/metabolism , Gene Expression Regulation, Plant , Plant Proteins/metabolism , Signal Transduction
4.
J Integr Plant Biol ; 58(3): 226-9, 2016 Mar.
Article in English | MEDLINE | ID: mdl-26619818

ABSTRACT

The long-distance signaling network allowing a plant to properly develop its root system is crucial to optimize root foraging in areas where nutrients are available. Cytokinin is an essential element of the systemic signaling network leading to the enhancement of lateral root proliferation in areas where nitrate is available. Here, we explore more precisely: (i) which particular traits of lateral root growth (density and length of emerged lateral roots) are the targets of systemic signaling in a context of heterogeneous nitrate supply; and (ii) if the systemic signaling depends only on cytokinin or on a combination of several signalings.


Subject(s)
Cytokinins/metabolism , Nitrates/metabolism , Signal Transduction , Arabidopsis/metabolism , Plant Roots/growth & development , Plant Roots/metabolism
5.
Plant Physiol ; 169(4): 2654-64, 2015 Dec.
Article in English | MEDLINE | ID: mdl-26446590

ABSTRACT

Nitrogen fixation in the legume-rhizobium symbiosis is a crucial area of research for more sustainable agriculture. Our knowledge of the plant cascade in response to the perception of bacterial Nod factors has increased in recent years. However, the discovery that Nod factors are not involved in the Aeschynomene-Bradyrhizobium spp. interaction suggests that alternative molecular dialogues may exist in the legume family. We evaluated the conservation of the signaling pathway common to other endosymbioses using three candidate genes: Ca(2+)/Calmodulin-Dependent Kinase (CCaMK), which plays a central role in cross signaling between nodule organogenesis and infection processes; and Symbiosis Receptor Kinase (SYMRK) and Histidine Kinase1 (HK1), which act upstream and downstream of CCaMK, respectively. We showed that CCaMK, SYMRK, and HK1 are required for efficient nodulation in Aeschynomene evenia. Our results demonstrate that CCaMK and SYMRK are recruited in Nod factor-independent symbiosis and, hence, may be conserved in all vascular plant endosymbioses described so far.


Subject(s)
Bradyrhizobium/physiology , Fabaceae/microbiology , Fabaceae/physiology , Plant Root Nodulation/physiology , Symbiosis/physiology , Amino Acid Sequence , Bradyrhizobium/metabolism , Calcium-Calmodulin-Dependent Protein Kinases/classification , Calcium-Calmodulin-Dependent Protein Kinases/genetics , Calcium-Calmodulin-Dependent Protein Kinases/metabolism , Fabaceae/genetics , Gene Expression Regulation, Plant , Histidine Kinase , Host-Pathogen Interactions , Lipopolysaccharides/metabolism , Microscopy, Confocal , Molecular Sequence Data , Phylogeny , Plant Proteins/classification , Plant Proteins/genetics , Plant Proteins/metabolism , Plant Root Nodulation/genetics , Plants, Genetically Modified , Protein Kinases/classification , Protein Kinases/genetics , Protein Kinases/metabolism , Receptor Protein-Tyrosine Kinases/genetics , Receptor Protein-Tyrosine Kinases/metabolism , Reverse Transcriptase Polymerase Chain Reaction , Sequence Homology, Amino Acid
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