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Phosphoproteomics Analysis of the Systemin Signaling Pathway

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EUR 49,90

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EUR 34,90

Phosphoproteomics Analysis of the Systemin Signaling Pathway (Band 12)

Fatima Haj Ahmad (Autor)

Vorschau

Leseprobe, PDF (1000 KB)
Inhaltsverzeichnis, PDF (660 KB)

ISBN-13 (Printausgabe) 9783736970465
ISBN-13 (E-Book) 9783736960466
Sprache Englisch
Seitenanzahl 190
Umschlagkaschierung glänzend
Auflage 1.
Buchreihe Schriftenreihe zur Physiologie und Biochemie der Pflanzen
Band 12
Erscheinungsort Göttingen
Promotionsort Hohenheim
Erscheinungsdatum 02.07.2019
Allgemeine Einordnung Dissertation
Fachbereiche Biologie
Botanik
Biochemie, Molekularbiologie, Gentechnologie
Schlagwörter Systemin,Biologie,Suspensionskultur
Beschreibung

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.