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Experimental study on the new significant function domains of KCHIP1 protein

Liu Xheng, Xiao Xiangjunn, Fan Feiyue, Sun Yuanming, Li Yumin, Yang Fujun

Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College. Tianjin 300192, China；Roy J. and Lucille A. Carver College of Medicine, The University of Iowa. USA

Abstract

Human Kv channel interacting protein 1 (KCHIP1) is a new member of the neural calcium binding protein superfamily. Theoretically KCHIP1 has several calcium binding domains and two myristoylation sites. In this study, we demonstrated that the calcium binding domains and myristoylation sites were functional. The first, through running SDS-PAGE gel, we testified its ability of binding Ca~(2+) with obvious discrepancy of the electrophoresis migrating rate after binding Ca~(2+). Then, through the techniques of fused green fluorescence protein and site-directed mutagenesis, we demonstrated that wild type KCHIP1 protein accumulated in the secretory vesicles of Golgi body. In contrast, its two mutated forms without myristoylation sites accumulated throughout the whole cytoplasm. These observations indicate that KCHIP1 protein has a myristoylation motif mediating the interaction between KCHIP1 protein and membrane.

Key words: Ca~(2+);Myristoylation;Site-directed mutagenesis

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Citing This Article：

Liu Xheng, Xiao Xiangjunn, Fan Feiyue, Sun Yuanming, Li Yumin, Yang Fujun. Experimental study on the new significant function domains of KCHIP1 protein. Acta Physiol Sin 2005; 57 (3): (in Chinese with English abstract).