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

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.

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Detalles Bibliográficos
Autores principales: Lin Bai, Amanda Kovach, Qinglong You, Hao-Chi Hsu, Gongpu Zhao, Huilin Li
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Q
Acceso en línea:https://doaj.org/article/e94c17af5f174b8bb315f2e32a1c2d9c
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Sumario: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.