An IQ domain mediates the interaction with calmodulin in a plant cyclic nucleotide-gated channel.

ABSTRACT: Cyclic nucleotide-gated channels (CNGCs) form non-selective cation entry pathways regulated by calmodulin (CaM), a universal Ca(2+) sensor in eukaryotes. Although CaM binding has been shown to be important for Ca(2+)-dependent feedback regulation of CNGC activity, the CaM-binding properties of these channels have been investigated in a few cases only. We show that CNGC20 from Arabidopsis thaliana binds CaM in a Ca(2+)-dependent manner and interacts with all AtCaM isoforms but not with the CaM-like proteins CML8 and CML9. CaM interaction with the full-length channel was demonstrated in planta, using bimolecular fluorescence complementation. This interaction occurred at the plasma membrane, in accordance with our localization data of green fluorescent protein (GFP)-fused CNGC20 proteins. The

SUBMITTER: Fischer C 

PROVIDER: S-EPMC3612182 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature