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Phosphoproteomics Analysis of the Systemin Signaling Pathway

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Phosphoproteomics Analysis of the Systemin Signaling Pathway (Volumen 12) (Tienda española)

Fatima Haj Ahmad (Autor)


Lectura de prueba, PDF (1000 KB)
Indice, PDF (660 KB)

ISBN-13 (Impresion) 9783736970465
ISBN-13 (E-Book) 9783736960466
Idioma Inglés
Numero de paginas 190
Laminacion de la cubierta Brillante
Edicion 1.
Serie Schriftenreihe zur Physiologie und Biochemie der Pflanzen
Volumen 12
Lugar de publicacion Göttingen
Lugar de la disertacion Hohenheim
Fecha de publicacion 02.07.2019
Clasificacion simple Tesis doctoral
Area Biología
Bioquímica, biología molecular, tecnología genética
Palabras claves Systemin,Biologie,Suspensionskultur

Systemin is a small peptide with important functions in plant wound response signaling. To elucidate systemin perception and signal transduction mechanisms, a phosphoproteomic profiling study was performed to reconstruct a systemin-specific kinase/phosphatase signaling network. Time course analyses revealed early events at the plasma membrane, such as dephosphorylation of H+-ATPase, and the phosphorylation of NADPH-oxidase and Ca2+-ATPase in response to systemin. Later responses included transient phosphorylation of small GTPases and vesicle trafficking proteins, as well as transcription factors. Based on a correlation analysis of systemin-induced phosphorylation profiles, substrate candidates for 44 systemin-responsive kinases and 9 phosphatases were predicted, some of which are involved in a regulatory circuit for the regulation of the plasma membrane H+-ATPase. In this regulatory model, H+-ATPase LHA1 is rapidly de-phosphorylated at its C-terminal regulatory residue T955 by phosphatase PLL5, resulting in the alkalization of the growth medium within two minutes of systemin treatment. LHA1 is re-activated by MAP-Kinase MPK2 later in the systemin response. A valuable resource of proteomic events involved in the systemin signaling cascade is provided with a focus on the prediction of substrates to early systemin-responsive kinases and phosphatases.