Cross-kingdom regulation of calcium- and/or calmodulin-dependent protein kinases by phospho-switches that relieve autoinhibition.

Melissa Bredow, Jacqueline Monaghan

Journal: Current opinion in plant biology 2022;68():102251

PMID: 35767936

Full Text on Elsevier Science View on PubMed

Abstract

Mechanisms to sense and respond to calcium have evolved in all organisms. Calmodulin is a universal calcium sensor across eukaryotes that directly binds calcium and associates with many downstream signal transducers including protein kinases. All eukaryotes encode calcium-dependent and/or calmodulin-dependent kinases, however there are distinct protein families across kingdoms. Here, we compare the activation mechanisms of calmodulin-dependent protein kinases (CaMKs), calcium- and calmodulin-dependent protein kinases (CCaMKs) and calcium-dependent protein kinases (CDPKs), noting striking similarities regarding phosphorylation in a regulatory segment known as the autoinhibitory junction. We thus propose that conserved regulation by phosphorylation underlies the activation of calcium-responsive proteins from different kingdoms.

Address: Department of Plant Pathology and Microbiology, Iowa State University, Ames IA, USA. Electronic address: [email protected].; Department of Biology, Queen's University, Kingston ON, Canada. Electronic address: [email protected].

DOI: 10.1016/j.pbi.2022.102251

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MeSH Terms: Calcium, Calcium-Calmodulin-Dependent Protein Kinases, Calmodulin, Phosphorylation, Protein Kinases