Functional role of EF-hands 3 and 4 in membrane-binding of KChIP1 |
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Authors: | Yan-Shun Liao Ku-Chung Chen Long-Sen Chang |
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Institution: | (1) Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan |
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Abstract: | The aim of the present study is to explore whether membrane targeting of K+ channel-interacting protein 1 (KChIP1) is associated with its EF-hand motifs and varies with specific phospholipids. Truncated
KChIP1, in which the EFhands 3 and 4 were deleted, retained the α-helix structure, indicating that the N-terminal half of KChIP1 could fold appropriately. Compared with wild-type KChIP1,
truncated KChIP1 exhibited lower lipid-binding capability. Compared with wild-type KChIP1, increasing membrane permeability
by the use of digitonin caused a marked loss of truncated KChIP1, suggesting that intact EF-hands 3 and 4 were crucial for
the anchorage of KChIP1 on membrane. KChIP1 showed a higher binding capability with phosphatidylserine (PS) than truncated
KChIP1. Unlike that of truncated KChIP1, the binding of wild-type KChIP1 with membrane was enhanced by increasing the PS content.
Moreover, the binding of KChIP1 with phospholipid vesicles induced a change in the structure of KChIP1 in the presence of
PS. Taken together, our data suggest that EF-hands 3 and 4 of KChIP1 are functionally involved in a specific association with
PS on the membrane. |
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Keywords: | EF-hand FTIR spectra KChIP1 lipid-binding |
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