Beyond PKA: Evolutionary and structural insights that define a docking and dimerization domain superfamily.

ABSTRACT: Protein-interaction domains can create unique macromolecular complexes that drive evolutionary innovation. By combining bioinformatic and phylogenetic analyses with structural approaches, we have discovered that the docking and dimerization (D/D) domain of the PKA regulatory subunit is an ancient and conserved protein fold. An archetypal function of this module is to interact with A-kinase-anchoring proteins (AKAPs) that facilitate compartmentalization of this key cell-signaling enzyme. Homology searching reveals that D/D domain proteins comprise a superfamily with 18 members that function in a variety of molecular and cellular contexts. Further in silico analyses indicate that D/D domains segregate into subgroups on the basis of their similarity to type I or type II PKA regulatory subunit

SUBMITTER: Dahlin HR 

PROVIDER: S-EPMC8339350 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature