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1.
Plant Cell Physiol ; 62(8): 1290-1301, 2021 Nov 10.
Artículo en Inglés | MEDLINE | ID: mdl-34059877

RESUMEN

Communication between plant cells and their biotic environment largely depends on the function of plasma membrane localized receptor-like kinases (RLKs). Major players in this communication within root meristems are secreted peptides, including CLAVATA3/EMBRYO SURROUNDING REGION40 (CLE40). In the distal root meristem, CLE40 acts through the RLK ARABIDOPSIS CRINKLY4 (ACR4) and the leucine-rich repeat (LRR) RLK CLAVATA1 (CLV1) to promote cell differentiation. In the proximal meristem, CLE40 signaling requires the LRR receptor-like protein CLAVATA2 (CLV2) and the membrane localized pseudokinase CORYNE (CRN) and serves to inhibit cell differentiation. The molecular components that act immediately downstream of the CLE40-activated receptors are not yet known. Here, we show that active CLE40 signaling triggers the release of intracellular Ca2+ leading to increased cytosolic Ca2+ concentration ([Ca2+]cyt) in a small subset of proximal root meristem cells. This rise in [Ca2+]cyt depends on the CYCLIC NUCLEOTIDE GATED CHANNELS (CNGCs) 6 and 9 and on CLV1. The precise function of changes in [Ca2+]cyt is not yet known but might form a central part of a fine-tuned response to CLE40 peptide that serves to integrate root meristem growth with stem cell fate decisions and initiation of lateral root primordia.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Calcio/metabolismo , Diferenciación Celular/efectos de los fármacos , Canales Catiónicos Regulados por Nucleótidos Cíclicos/metabolismo , Meristema/metabolismo , Raíces de Plantas/metabolismo , Arabidopsis/genética , Proteínas de Arabidopsis/genética , Diferenciación Celular/genética , Canales Catiónicos Regulados por Nucleótidos Cíclicos/genética , Variación Genética , Genotipo , Meristema/genética , Raíces de Plantas/genética , Transducción de Señal/efectos de los fármacos , Transducción de Señal/genética
2.
Proc Natl Acad Sci U S A ; 115(13): 3488-3493, 2018 03 27.
Artículo en Inglés | MEDLINE | ID: mdl-29531026

RESUMEN

Plant-unique membrane receptor kinases with leucine-rich repeat ectodomains (LRR-RKs) can sense small molecule, peptide, and protein ligands. Many LRR-RKs require SERK-family coreceptor kinases for high-affinity ligand binding and receptor activation. How one coreceptor can contribute to the specific binding of distinct ligands and activation of different LRR-RKs is poorly understood. Here we quantitatively analyze the contribution of SERK3 to ligand binding and activation of the brassinosteroid receptor BRI1 and the peptide hormone receptor HAESA. We show that while the isolated receptors sense their respective ligands with drastically different binding affinities, the SERK3 ectodomain binds the ligand-associated receptors with very similar binding kinetics. We identify residues in the SERK3 N-terminal capping domain, which allow for selective steroid and peptide hormone recognition. In contrast, residues in the SERK3 LRR core form a second, constitutive receptor-coreceptor interface. Genetic analyses of protein chimera between BRI1 and SERK3 define that signaling-competent complexes are formed by receptor-coreceptor heteromerization in planta. A functional BRI1-HAESA chimera suggests that the receptor activation mechanism is conserved among different LRR-RKs, and that their signaling specificity is encoded in the kinase domain of the receptor. Our work pinpoints the relative contributions of receptor, ligand, and coreceptor to the formation and activation of SERK-dependent LRR-RK signaling complexes regulating plant growth and development.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Proteínas Quinasas/metabolismo , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas/metabolismo , Receptores de Superficie Celular/metabolismo , Arabidopsis/crecimiento & desarrollo , Proteínas de Arabidopsis/química , Cinética , Proteínas Repetidas Ricas en Leucina , Ligandos , Desarrollo de la Planta , Unión Proteica , Conformación Proteica , Proteínas Quinasas/química , Proteínas Serina-Treonina Quinasas/química , Proteínas/química , Receptores de Superficie Celular/química , Transducción de Señal
3.
Plant Physiol ; 173(2): 1146-1163, 2017 02.
Artículo en Inglés | MEDLINE | ID: mdl-27994007

RESUMEN

The plant cuticle is laid down at the cell wall surface of epidermal cells in a wide variety of structures, but the functional significance of this architectural diversity is not yet understood. Here, the structure-function relationship of the petal cuticle of Arabidopsis (Arabidopsis thaliana) was investigated. Applying Fourier transform infrared microspectroscopy, the cutin mutants long-chain acyl-coenzyme A synthetase2 (lacs2), permeable cuticle1 (pec1), cyp77a6, glycerol-3-phosphate acyltransferase6 (gpat6), and defective in cuticular ridges (dcr) were grouped in three separate classes based on quantitative differences in the ν(C=O) and ν(C-H) band vibrations. These were associated mainly with the quantity of 10,16-dihydroxy hexadecanoic acid, a monomer of the cuticle polyester, cutin. These spectral features were linked to three different types of cuticle organization: a normal cuticle with nanoridges (lacs2 and pec1 mutants); a broad translucent cuticle (cyp77a6 and dcr mutants); and an electron-opaque multilayered cuticle (gpat6 mutant). The latter two types did not have typical nanoridges. Transmission electron microscopy revealed considerable variations in cuticle thickness in the dcr mutant. Different double mutant combinations showed that a low amount of C16 monomers in cutin leads to the appearance of an electron-translucent layer adjacent to the cuticle proper, which is independent of DCR action. We concluded that DCR is not only essential for incorporating 10,16-dihydroxy C16:0 into cutin but also plays a crucial role in the organization of the cuticle, independent of cutin composition. Further characterization of the mutant petals suggested that nanoridge formation and conical cell shape may contribute to the reduction of physical adhesion forces between petals and other floral organs during floral development.


Asunto(s)
Arabidopsis/fisiología , Arabidopsis/ultraestructura , Flores/fisiología , Flores/ultraestructura , Lípidos de la Membrana/química , Epidermis de la Planta/ultraestructura , Adhesividad , Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Forma de la Célula , Pared Celular/metabolismo , Pared Celular/ultraestructura , Flores/citología , Genotipo , Modelos Biológicos , Mutación/genética , Ácidos Palmíticos/metabolismo , Pectinas/metabolismo , Espectroscopía Infrarroja por Transformada de Fourier
4.
Annu Rev Plant Biol ; 70: 153-186, 2019 04 29.
Artículo en Inglés | MEDLINE | ID: mdl-30525926

RESUMEN

During the past decade, a flurry of research focusing on the role of peptides as short- and long-distance signaling molecules in plant cell communication has been undertaken. Here, we focus on peptides derived from nonfunctional precursors, and we address several key questions regarding peptide signaling. We provide an overview of the regulatory steps involved in producing a biologically active peptide ligand that can bind its corresponding receptor(s) and discuss how this binding and subsequent activation lead to specific cellular outputs. We discuss different experimental approaches that can be used to match peptide ligands with their receptors. Lastly, we explore how peptides evolved from basic signaling units regulating essential processes in plants to more complex signaling systems as new adaptive traits developed and how nonplant organisms exploit this signaling machinery by producing peptide mimics.


Asunto(s)
Péptidos , Plantas , Ligandos , Transducción de Señal
6.
Nat Plants ; 4(8): 596-604, 2018 08.
Artículo en Inglés | MEDLINE | ID: mdl-30061750

RESUMEN

The root cap protects the stem cell niche of angiosperm roots from damage. In Arabidopsis, lateral root cap (LRC) cells covering the meristematic zone are regularly lost through programmed cell death, while the outermost layer of the root cap covering the tip is repeatedly sloughed. Efficient coordination with stem cells producing new layers is needed to maintain a constant size of the cap. We present a signalling pair, the peptide IDA-LIKE1 (IDL1) and its receptor HAESA-LIKE2 (HSL2), mediating such communication. Live imaging over several days characterized this process from initial fractures in LRC cell files to full separation of a layer. Enhanced expression of IDL1 in the separating root cap layers resulted in increased frequency of sloughing, balanced with generation of new layers in a HSL2-dependent manner. Transcriptome analyses linked IDL1-HSL2 signalling to the transcription factors BEARSKIN1/2 and genes associated with programmed cell death. Mutations in either IDL1 or HSL2 slowed down cell division, maturation and separation. Thus, IDL1-HSL2 signalling potentiates dynamic regulation of the homeostatic balance between stem cell division and sloughing activity.


Asunto(s)
Proteínas de Arabidopsis/fisiología , Arabidopsis/metabolismo , Péptidos y Proteínas de Señalización Intercelular/fisiología , Arabidopsis/citología , Arabidopsis/crecimiento & desarrollo , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , División Celular/genética , Pared Celular/metabolismo , Perfilación de la Expresión Génica , Homeostasis , Péptidos y Proteínas de Señalización Intercelular/genética , Péptidos y Proteínas de Señalización Intercelular/metabolismo , Meristema/citología , Meristema/genética , Meristema/metabolismo , Raíces de Plantas/citología , Raíces de Plantas/metabolismo , Raíces de Plantas/fisiología , Proteínas Serina-Treonina Quinasas/genética , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Serina-Treonina Quinasas/fisiología , Señales de Clasificación de Proteína/fisiología , Transducción de Señal
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