The calcineurin signaling network evolves via conserved kinase-phosphatase modules that transcend substrate identity.

ABSTRACT: To define a functional network for calcineurin, the conserved Ca(2+)/calmodulin-regulated phosphatase, we systematically identified its substrates in S. cerevisiae using phosphoproteomics and bioinformatics, followed by copurification and dephosphorylation assays. This study establishes new calcineurin functions and reveals mechanisms that shape calcineurin network evolution. Analyses of closely related yeasts show that many proteins were recently recruited to the network by acquiring a calcineurin-recognition motif. Calcineurin substrates in yeast and mammals are distinct due to network rewiring but, surprisingly, are phosphorylated by similar kinases. We postulate that corecognition of conserved substrate features, including phosphorylation and docking motifs, preserves calcineurin-kinas

SUBMITTER: Goldman A 

PROVIDER: S-EPMC4127121 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature