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Phosphoproteomics Analysis of the Systemin Signaling Pathway

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Phosphoproteomics Analysis of the Systemin Signaling Pathway (Volume 12) (English shop)

Fatima Haj Ahmad (Author)


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Table of Contents, PDF (660 KB)

ISBN-13 (Hard Copy) 9783736970465
ISBN-13 (eBook) 9783736960466
Language English
Page Number 190
Lamination of Cover glossy
Edition 1.
Book Series Schriftenreihe zur Physiologie und Biochemie der Pflanzen
Volume 12
Publication Place Göttingen
Place of Dissertation Hohenheim
Publication Date 2019-07-02
General Categorization Dissertation
Departments Biology
Biochemistry, molecular biology, gene technology
Keywords 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.