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BioMed Central, Cell Communication and Signaling, 1(12), 2014

DOI: 10.1186/s12964-014-0060-z

BioMed Central, Cell Communication and Signaling, 1(12), p. 60

DOI: 10.1186/preaccept-3431251013169955

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Calcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1

Journal article published in 2014 by Victor Muleya ORCID, Janet I. Wheeler, Oziniel Ruzvidzo, Lubna Freihat, David T. Manallack, Christoph A. Gehring ORCID, Helen R. Irving
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Abstract Background A number of receptor kinases contain guanylate cyclase (GC) catalytic centres encapsulated in the cytosolic kinase domain. A prototypical example is the phytosulfokine receptor 1 (PSKR1) that is involved in regulating growth responses in plants. PSKR1 contains both kinase and GC activities however the underlying mechanisms regulating the dual functions have remained elusive. Findings Here, we confirm the dual activity of the cytoplasmic domain of the PSKR1 receptor. We show that mutations within the guanylate cyclase centre modulate the GC activity while not affecting the kinase catalytic activity. Using physiologically relevant Ca 2+ levels, we demonstrate that its GC activity is enhanced over two-fold by Ca 2+ in a concentration-dependent manner. Conversely, increasing Ca 2+ levels inhibits kinase activity up to 500-fold at 100 nM Ca 2+ . Conclusions Changes in calcium at physiological levels can regulate the kinase and GC activities of PSKR1. We therefore propose a functional model of how calcium acts as a bimodal switch between kinase and GC activity in PSKR1 that could be relevant to other members of this novel class of ligand-activated receptor kinases.