Publication in refereed journal
香港中文大学研究人员 ( 现职)
| 韦妙宜教授 (那打素护理学院) |
| 李卓予教授 (生物医学学院) |
| 冯国培教授 (生物医学学院) |
| 徐国荣教授 (生物医学学院) |
| 李铭源博士 |
| 倪世明教授 (生命科学学院) |
全文
| 数位物件识别号 (DOI) http://dx.doi.org/10.1002/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-I |
引用次数
Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/38WOS source URL
其它资讯
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.
着者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
期刊名称Journal of Cellular Biochemistry
出版年份2000
月份1
日期1
卷号78
期次4
出版社WILEY-LISS
页次558 - 565
国际标準期刊号0730-2312
电子国际标準期刊号1097-4644
语言英式英语
关键词alpha-actinin 2; LIM domain; PDZ domain; yeast two-hybrid screening
Web of Science 学科类别Biochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Cell Biology; CELL BIOLOGY
