I am studying the regulation of the C. elegans IP3 receptor (IP3R) in vivo. The IP3R has numerous predicted protein binding and modification sites, and determining how they modify the action of the channel may be crucial to our understanding of how calcium signalling achieves its exquisite diversity and specificity.
Although most protein interaction studies have been performed on mammalian IP3Rs (specifically IP3R1 and, to a lesser extent, IP3R3), many of the predicted binding sites are conserved between mammals and C. elegans. This allows us to study interactions in a well-characterised and simple model system, while retaining all the relevance of in vivo study.
Previous work on the proposed interaction between IP3R and the immunophilin protein FKBP12 suggested that the homologue of the binding site for FKBP12 may have functional relevance in C. elegans. I am using a variety of molecular approaches to analyse the interaction between these two proteins and the effect of itr-1-mediated phenotypes in vivo.
I am also using a suppressor mapping approach to identify novel interactions with itr-1.