Experimental study on the new significant function domains of KCHIP1 protein.
- Author:
Zheng LIU
1
;
Xiang-Jun XIAO
;
Fei-Yue FAN
;
Yuan-Ming SUN
;
Yu-Min LI
;
Fu-Jun YANG
Author Information
1. Institute of Radiation Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, Tianjin 300192, China. liuzheng19752002@yahoo.com.cn
- Publication Type:Journal Article
- MeSH:
Animals;
COS Cells;
Calcium;
metabolism;
Calcium-Binding Proteins;
genetics;
metabolism;
Cercopithecus aethiops;
Humans;
Kv Channel-Interacting Proteins;
chemistry;
physiology;
Potassium Channels;
metabolism;
Potassium Channels, Voltage-Gated;
metabolism;
Protein Transport;
Recombinant Fusion Proteins;
metabolism;
Transfection
- From:
Acta Physiologica Sinica
2005;57(3):346-348
- CountryChina
- Language:English
-
Abstract:
Human K(v) 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.
