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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/034/02/0203-0211

    • Keywords

       

      EF-hand; FTIR spectra; KChIP1; lipid-binding

    • 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 EF-hands 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.

    • Author Affiliations

       

      Yan-Shun Liao1 Ku-Chung Chen1 Long-Sen Chang1

      1. Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan
    • Dates

       
  • Journal of Biosciences | News

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