Variation in assembly stoichiometry in non-metazoan homologs of the hub domain of Ca²⁺ /calmodulin-dependent protein kinase II.

ABSTRACT: The multi-subunit Ca²⁺ /calmodulin-dependent protein kinase II (CaMKII) holoenzyme plays a critical role in animal learning and memory. The kinase domain of CaMKII is connected by a flexible linker to a C-terminal hub domain that assembles into a 12- or 14-subunit scaffold that displays the kinase domains around it. Studies on CaMKII suggest that the stoichiometry and dynamic assembly/disassembly of hub oligomers may be important for CaMKII regulation. Although CaMKII is a metazoan protein, genes encoding predicted CaMKII-like hub domains, without associated kinase domains, are found in the genomes of some green plants and bacteria. We show that the hub domains encoded by three related green algae, Chlamydomonas reinhardtii, Volvox carteri f. nagarensis, and Gonium pectoral, ass

SUBMITTER: McSpadden ED 

PROVIDER: S-EPMC6511747 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature