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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-06

AUTHORS

Yan-Shun Liao, Ku-Chung Chen, Long-Sen Chang

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. More... »

PAGES

203-211

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12038-009-0024-4

DOI

http://dx.doi.org/10.1007/s12038-009-0024-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034043748

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19550036


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