Interaction of hCLIM1, an Enigma family protein, with alpha-actinin 2
Publication in refereed journal


摘要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 alpha-actinin 2, the skeletal muscle isoform of alpha-actinin. hCLIM1 protein was shown to interact with alpha-actinin 2 by yeast two-hybrid screening and immunochemical analyses. Yeast two-hybrid analyses also demonstrated that the FIM domain of hCLIM1 binds to the EF-hand region of alpha-actinin 2, defining a new mode of LIM domain interactions. Immunofluorescent study demonstrates that hCLIM1 colocalizes with alpha-actinin at the Z-disks in human myocardium. Taken together, our experimental results suggest that hCLIM1 is a novel cytoskeletal protein and may act as an adapter that brings other proteins to the cytoskeleton. J. Cell. Biochem. 78:558-565, 2000. (C) 2000 Wiley-Liss, Inc.
著者Kotaka M, Kostin S, Ngai S, Chan K, Lau Y, Lee SMY, Li H, Ng EKO, Schaper J, Tsui SKW, Fung K, Lee C, Waye MMY
期刊名稱Journal of Cellular Biochemistry
頁次558 - 565
關鍵詞alpha-actinin 2; LIM domain; PDZ domain; yeast two-hybrid screening
Web of Science 學科類別Biochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Cell Biology; CELL BIOLOGY

上次更新時間 2020-09-08 於 06:41