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Verfasst von:Oppermann, Felix Sebastian [VerfasserIn]   i
 Gruss, Oliver [VerfasserIn]   i
Titel:Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets
Verf.angabe:Felix S. Oppermann, Kathrin Grundner-Culemann, Chanchal Kumar, Oliver J. Gruss, Prasad V. Jallepalli, and Henrik Daub
Jahr:2012
Jahr des Originals:2011
Umfang:12 S.
Teil:volume:11
 year:2012
 number:4
 extent:12
Fussnoten:Gesehen am 19.10.2018 ; Published online: Dec 22, 2011
Titel Quelle:Enthalten in: Molecular & cellular proteomics
Ort Quelle:Bethesda, Md. : The American Society for Biochemistry and Molecular Biology, 2002
Jahr Quelle:2012
Band/Heft Quelle:11(2012), 4
ISSN Quelle:1535-9484
Abstract:Delineation of phosphorylation-based signaling networks requires reliable data about the underlying cellular kinase-substrate interactions. We report a chemical genetics and quantitative phosphoproteomics approach that encompasses cellular kinase activation in combination with comparative replicate mass spectrometry analyses of cells expressing either inhibitor-sensitive or resistant kinase variant. We applied this workflow to Plk1 (Polo-like kinase 1) in mitotic cells and induced cellular Plk1 activity by wash-out of the bulky kinase inhibitor 3-MB-PP1, which targets a mutant kinase version with an enlarged catalytic pocket while not interfering with wild-type Plk1. We quantified more than 20,000 distinct phosphorylation sites by SILAC, approximately half of which were measured in at least two independent experiments in cells expressing mutant and wild-type Plk1. Based on replicate phosphorylation site quantifications in both mutant and wild-type Plk1 cells, our chemical genetic proteomics concept enabled stringent comparative statistics by significance analysis of microarrays, which unveiled more than 350 cellular downstream targets of Plk1 validated by full concordance of both statistical and experimental data. Our data point to hitherto poorly characterized aspects in Plk1-controlled mitotic progression and provide a largely extended resource for functional studies. We anticipate the described strategies to be of general utility for systematic and confident identification of cellular protein kinase substrates.
DOI:doi:10.1074/mcp.O111.012351
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: http://dx.doi.org/10.1074/mcp.O111.012351
 Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3322579/
 DOI: https://doi.org/10.1074/mcp.O111.012351
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1582108129
Verknüpfungen:→ Zeitschrift

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