BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases.

Fischer C, Sauter M, Dietrich P (2017)

Publication Language: English

Publication Status: Published

Publication Type: Journal article, Original article

Publication year: 2017

Journal

Methods in Molecular Biology Humana Press

Book Volume: 1621

Pages Range: 141-149

DOI: 10.1007/978-1-4939-7063-6_14

Abstract

Plant receptor-like kinases (RLKs) are regulated at various levels including posttranscriptional modification and interaction with regulatory proteins. Calmodulin (CaM) is a calcium-sensing protein that was shown to bind to some RLKs such as the PHYTOSULFOKINE RECEPTOR1 (PSKR1). The CaM-binding site is embedded in subdomain VIa of the kinase domain. It is possible that many more of RLKs interact with CaM than previously described. To unequivocally confirm CaM binding, several methods exist. Bimolecular fluorescence complementation (BiFC) and pull-down assays have been successfully used to study CaM binding to PSKR1 and are described in this chapter (BiFC) and in Chapter 15 (pull down). The two methods are complementary. BiFC is useful to show localization and interaction of soluble as well as of membrane-bound proteins in planta.

Authors with CRIS profile

Cornelia Fischer Professur für Zellbiologie der Pflanzen Petra Dietrich Professur für Zellbiologie der Pflanzen

Involved external institutions

Christian-Albrechts-Universität zu Kiel DE Germany (DE)

How to cite

APA:

Fischer, C., Sauter, M., & Dietrich, P. (2017). BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases. Methods in Molecular Biology, 1621, 141-149. https://dx.doi.org/10.1007/978-1-4939-7063-6_14

MLA:

Fischer, Cornelia, Margret Sauter, and Petra Dietrich. "BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases." Methods in Molecular Biology 1621 (2017): 141-149.

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