Autoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p

Lin Bai; Amanda Kovach; Qinglong You; Hao-Chi Hsu; Gongpu Zhao; Huilin Li

doi:10.1038/s41467-019-12191-9

Nature Communications (Sep 2019)

Autoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p

Lin Bai,
Amanda Kovach,
Qinglong You,
Hao-Chi Hsu,
Gongpu Zhao,
Huilin Li

Affiliations

Lin Bai: Structural Biology Program, Van Andel Research Institute
Amanda Kovach: Structural Biology Program, Van Andel Research Institute
Qinglong You: Structural Biology Program, Van Andel Research Institute
Hao-Chi Hsu: Structural Biology Program, Van Andel Research Institute
Gongpu Zhao: David Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute
Huilin Li: Structural Biology Program, Van Andel Research Institute

DOI: https://doi.org/10.1038/s41467-019-12191-9
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

Read online

The heterodimeric eukaryotic Drs2p-Cdc50p complex is a lipid flippase that maintains cell membrane asymmetry and its autoinhibition is released by PI4P binding. Here authors show cryo-EM structures of Drs2p-Cdc50p in apo and PI4P-activated form which reveal the structural changes upon PI4P binding.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal