Calcium/Calmodulin-dependent protein kinase is negatively and positively regulated by calcium, providing a mechanism for decoding calcium responses during symbiosis signaling

Miller, J Benjamin ORCID: https://orcid.org/0000-0003-0882-033X, Pratap, Amitesh, Miyahara, Akira, Zhou, Liang, Bornemann, Stephen, Morris, Richard J and Oldroyd, Giles E D (2013) Calcium/Calmodulin-dependent protein kinase is negatively and positively regulated by calcium, providing a mechanism for decoding calcium responses during symbiosis signaling. The Plant Cell, 25 (12). pp. 5053-5066. ISSN 1040-4651

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Abstract

The establishment of symbiotic associations in plants requires calcium oscillations that must be decoded to invoke downstream developmental programs. In animal systems, comparable calcium oscillations are decoded by calmodulin (CaM)-dependent protein kinases, but symbiotic signaling involves a calcium/CaM-dependent protein kinase (CCaMK) that is unique to plants. CCaMK differs from the animal CaM kinases by its dual ability to bind free calcium, via calcium binding EF-hand domains on the protein, or to bind calcium complexed with CaM, via a CaM binding domain. In this study, we dissect this dual regulation of CCaMK by calcium. We find that calcium binding to the EF-hand domains promotes autophosphorylation, which negatively regulates CCaMK by stabilizing the inactive state of the protein. By contrast, calcium-dependent CaM binding overrides the effects of autophosphorylation and activates the protein. The differential calcium binding affinities of the EF-hand domains compared with those of CaM suggest that CCaMK is maintained in the inactive state at basal calcium concentrations and is activated via CaM binding during calcium oscillations. This work provides a model for decoding calcium oscillations that uses differential calcium binding affinities to create a robust molecular switch that is responsive to calcium concentrations associated with both the basal state and with oscillations.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009) Faculty of Science > School of Computing Sciences Faculty of Science > School of Mathematics (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	30 Jul 2015 14:40
Last Modified:	25 Sep 2024 11:52
URI:	https://ueaeprints.uea.ac.uk/id/eprint/53553
DOI:	10.1105/tpc.113.116921

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