Phosphorylation of S344 in the calmodulin-binding domain negatively affects CCaMK function during bacterial and fungal symbioses

Author:

Routray Pratyush,Miller J. Benjamin1,Du Liqun,Oldroyd Giles1,Poovaiah B. W.

Affiliation:

1. Department of Cell & Developmental Biology; John Innes Centre; Norwich; NR4 7UH; UK

Publisher

Wiley

Subject

Cell Biology,Plant Science,Genetics

Reference40 articles.

1. Divergence of evolutionary ways among common sym genes: CASTOR and CCaMK show functional conservation between two symbiosis systems and constitute the root of a common signaling pathway;Banba;Plant Cell Physiol.,2008

2. Agrobacterium rhizogenes-transformed roots of Medicago truncatula for the study of nitrogen-fixing and endomycorrhizal symbiotic associations;Boisson-Dernier;Mol. Plant-Microbe Interact.,2001

3. OsIPD3, an ortholog of the Medicago truncatula DMI3 interacting protein IPD3, is required for mycorrhizal symbiosis in rice;Chen;New Phytol.,2008

4. Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. Studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides;Colbran;J. Biol. Chem.,1990

5. Breaking the code: Ca2+ sensors in plant signalling;DeFalco;Biochem. J.,2010

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