Structural basis for the membrane association of ankyrinG via palmitoylation

Yuichiro Fujiwara, Hiroko X. Kondo, Matsuyuki Shirota, Megumi Kobayashi, Kohei Takeshita, Atsushi Nakagawa, Yasushi Okamura, Kengo Kinoshita

研究成果: Article査読

9 被引用数 (Scopus)


By clustering various ion channels and transporters, ankyrin-G (AnkG) configures the membrane-excitation 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 coarse-grained 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.

ジャーナルScientific reports
出版ステータスPublished - 2016 4 5

ASJC Scopus subject areas

  • 一般


「Structural basis for the membrane association of ankyrinG via palmitoylation」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。