Functional role of EF-hands 3 and 4 in membrane-binding of KChIP1

Yan Shun Liao, Ku Chung Chen, Long Sen Chang

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)203-211
Number of pages9
JournalJournal of Biosciences
Volume34
Issue number2
DOIs
Publication statusPublished - Jun 2009
Externally publishedYes

Keywords

  • EF-hand
  • FTIR spectra
  • KChIP1
  • Lipid-binding

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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