Interaction of hCLIM1, an enigma family protein, with ?-actinin 2

Publisher Website
Google Scholar
Abstract
Enigma proteins are proteins that possess a PDZ domain at the amino terminal and one to three LIM domains at the carboxyl terminal. They are cytoplasmic proteins that are involved with the cytoskeleton and signal transduction pathway. By virtue of the two protein interacting domains, they are capable of protein-protein interactions. Here we report a study on a human Enigma protein hCLIM1, in particular. Our study describes the interaction of the human 36kDa carboxyl terminal LIM domain protein (hCLIM1), the human homologue of CLP36 in rat, with α-actinin 2, the skeletal muscle isoform of α-actinin. hCLIM1 protein was shown to interact with α-actinin 2 by yeast two-hybrid screening and immunochemical analyses. Yeast two-hybrid analyses also demonstrated that the LIM domain of hCLIM1 binds to the EF-hand region of α-actinin 2, defining a new mode of LIM domain interactions. Immunofluorescent study demonstrates that hCLIM1 colocalizes with α-actinin at the Z-disks in human myocardium. Taken together, our experimental results suggest that hCLIM1is a novel cytoskeletal protein and may act as an adapter that brings other proteins to the cytoskeleton. J. Cell. Biochem. 78:558–565, 2000.