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Deciphering the Symbiotic Calcium Code: The activation of CCaMK

Reference	BBS/E/J/000CA496
Principal Investigator / Supervisor	Professor Richard Morris
Co-Investigators / Co-Supervisors	Professor Stephen Bornemann, Professor Giles Oldroyd
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	293,613
Status	Completed
Type	Institute Project
Start date	07/01/2013
End date	06/07/2016
Duration	41 months

Abstract

Calcium oscillations are known to play a key role in nodulation. However, it is not known how calcium changes activate downstream events that give rise to this important developmental programme. Mycorrhization shares many components of the nodulation pathway, in fact, the nodulation pathway likely evolved from the former. The activation of a calcium and calmodulin dependent protein kinase, CCaMK, is necessary for both processes and genetic studies suggest that the pathways diverge at this point. Within the proposed research programme, we wish to exploit recent advances in location specific cameleon lines that we have engineered into M. truncatula, developments in high resolution confocal imaging, and stochastic spatio-temporal modelling to build 3D models of signal generation on realistic geometries in order to determine the calcium concentration profiles that CCaMK is exposed to. We will reconstruct the spatiotemporal patterns observed in and around the nucleus solving a number of plausible models (CICR, voltage-gated, ligand-gated channels) on realistic geometries using the fire-diffuse-fire framework. These models will be parameterised by values derived from a statistical analysis of confocal images of fine slices of the nuclear membrane. Proteomic approaches will be employed to determine the concentrations of CCaMK and calmodulin (Cam). We will use label-free quantification as our primary method of measuring the abundance of CCaMK and CaM in root hairs. This information will be combined with detailed studies on the phosphorylation dynamics of key residues within CCaMK as a function of calcium concentration and the kinetics of calcium and calmodulin binding to unravel the mode of activation of CCaMK and the decoding strategy.

Summary

unavailable

Committee	Not funded via Committee
Research Topics	Plant Science
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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