Cryo-EM structure of TMEM16F in digitonin without calcium bound
Ontology highlight
ABSTRACT:
SUBMITTER: Shangyu Dang
PROVIDER: EMPIAR-10279 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM Studies of TMEM16F Calcium-Activated Ion Channel Suggest Features Important for Lipid Scrambling.
Feng Shengjie S Dang Shangyu S Han Tina Wei TW Ye Wenlei W Jin Peng P Cheng Tong T Li Junrui J Jan Yuh Nung YN Jan Lily Yeh LY Cheng Yifan Y
Cell reports 20190701 2
As a Ca<sup>2+</sup>-activated lipid scramblase and ion channel that mediates Ca<sup>2+</sup> influx, TMEM16F relies on both functions to facilitate extracellular vesicle generation, blood coagulation, and bone formation. How a bona fide ion channel scrambles lipids remains elusive. Our structural analyses revealed the coexistence of an intact channel pore and PIP<sub>2</sub>-dependent protein conformation changes leading to membrane distortion. Correlated to the extent of membrane distortion, m ...[more]
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