Developmentally regulated alternative splicing of densin modulates protein-protein interaction and subcellular localization.

ABSTRACT: Densin is a member of the leucine-rich repeat (LRR) and PDZ domain (LAP) protein family that binds several signaling molecules via its C-terminal domains, including calcium/calmodulin-dependent protein kinase II (CaMKII). In this study, we identify several novel mRNA splice variants of densin that are differentially expressed during development. The novel variants share the LRR domain but are either prematurely truncated or contain internal deletions relative to mature variants of the protein (180 kDa), thus removing key protein-protein interaction domains. For example, CaMKIIalpha coimmunoprecipitates with densin splice variants containing an intact C-terminal domain from lysates of transfected HEK293 cells, but not with variants that only contain N-terminal domains. Immunoblot analyses u

SUBMITTER: Jiao Y 

PROVIDER: S-EPMC2814316 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature