Publikation: Detection of Phosphorylation on Immunoprecipitates from Total Protein Extracts of Arabidopsis thaliana Seedlings
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2020
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OTEGUI, Marisa S., ed.. Plant Endosomes : Methods and Protocols. 2nd edition. New York, NY: Humana Press, 2020, pp. 169-182. Methods in Molecular Biology. 2177. ISBN 978-1-07-160766-4. Available under: doi: 10.1007/978-1-0716-0767-1_14
Zusammenfassung
Phosphorylation is a versatile posttranslational modification that can regulate the localization, stability, and conformation of proteins; protein-protein interactions; and enzyme activities. Phosphorylation of plasma membrane proteins, for example, can serve as recognition signals for ubiquitin ligases and hence can trigger its endocytic degradation. Key determinants of protein phosphorylation are kinases and phosphatases that are spatiotemporally regulated to phosphorylate or dephosphorylate specific target proteins. To understand the dynamics and regulatory mechanisms of protein phosphorylation, it is essential to analyze the phosphorylation status of the proteins and identify phosphorylation sites as well as the modifying enzymes. In this chapter, we describe methods that can be used for the detection of phosphoproteins that are immunoprecipitated from Arabidopsis total extracts.
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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Immunoprecipitation, Protein phosphorylation, Phosphostain, Phos-Tag™ gel
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VOGEL, Karin, Erika ISONO, 2020. Detection of Phosphorylation on Immunoprecipitates from Total Protein Extracts of Arabidopsis thaliana Seedlings. In: OTEGUI, Marisa S., ed.. Plant Endosomes : Methods and Protocols. 2nd edition. New York, NY: Humana Press, 2020, pp. 169-182. Methods in Molecular Biology. 2177. ISBN 978-1-07-160766-4. Available under: doi: 10.1007/978-1-0716-0767-1_14BibTex
@incollection{Vogel2020Detec-51146,
year={2020},
doi={10.1007/978-1-0716-0767-1_14},
title={Detection of Phosphorylation on Immunoprecipitates from Total Protein Extracts of Arabidopsis thaliana Seedlings},
edition={2nd edition},
number={2177},
isbn={978-1-07-160766-4},
publisher={Humana Press},
address={New York, NY},
series={Methods in Molecular Biology},
booktitle={Plant Endosomes : Methods and Protocols},
pages={169--182},
editor={Otegui, Marisa S.},
author={Vogel, Karin and Isono, Erika}
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<dcterms:abstract xml:lang="eng">Phosphorylation is a versatile posttranslational modification that can regulate the localization, stability, and conformation of proteins; protein-protein interactions; and enzyme activities. Phosphorylation of plasma membrane proteins, for example, can serve as recognition signals for ubiquitin ligases and hence can trigger its endocytic degradation. Key determinants of protein phosphorylation are kinases and phosphatases that are spatiotemporally regulated to phosphorylate or dephosphorylate specific target proteins. To understand the dynamics and regulatory mechanisms of protein phosphorylation, it is essential to analyze the phosphorylation status of the proteins and identify phosphorylation sites as well as the modifying enzymes. In this chapter, we describe methods that can be used for the detection of phosphoproteins that are immunoprecipitated from Arabidopsis total extracts.</dcterms:abstract>
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