学術雑誌論文

学術雑誌論文

text

Scientific Reports. 2016, 6, p. 23981

Structural basis for the membrane association of ankyrinG via palmitoylation

Springer Nature

英語

text

2016-04

https://doi.org/10.1038/srep23981

Fujiwara, Y., Kondo, H., Shirota, M. et al. Structural basis for the membrane association of ankyrinG via palmitoylation. Sci Rep 6, 23981 (2016) doi:10.1038/srep23981

By clustering various ion channels and transporters, ankyrin-G (AnkG) configures the membraneexcitation platforms in neurons and cardiomyocytes. AnkG itself localizes to specific areas on the plasma membrane via s-palmitoylation of Cys. However, the structural mechanism by which AnkG anchors to the membrane is not understood. In this study, we solved the crystal structures of the reduced and oxidized forms of the AnkG s-palmitoylation domain and used multiple long-term coarsegrained molecular dynamics simulations to analyze their membrane association. Here we report that the membrane anchoring of AnkG was facilitated by s-palmitoylation, defining a stable binding interface on the lipid membrane, and that AnkG without s-palmitoylation also preferred to stay near the membrane but did not have a unique binding interface. This suggests that AnkG in the juxtamembrane region is primed to accept lipid modification at Cys, and once that happens AnkG constitutes a rigid structural base upon which a membrane-excitation platform can be assembled.

© 2016 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.

73667

Structural basis for the membrane association of ankyrinG via palmitoylation

Springer Nature

英語

2016-04

Scientific Reports

6

23981

https://doi.org/10.1038/srep23981

27046665

https://hdl.handle.net/11094/73667