Myr-Arf1 conformational flexibility at the membrane surface sheds light on the interactions with ArfGAP ASAP1

Abstract ADP-ribosylation factor 1 (Arf1) interacts with multiple cellular partners and membranes to regulate intracellular traffic, organelle structure and actin dynamics. Defining the dynamic conformational landscape of Arf1 in its active form, when bound to the membrane, is of high functional rel...

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Bibliographic Details
Published in:Nature Communications
Main Authors: Yue Zhang, Olivier Soubias, Shashank Pant, Frank Heinrich, Alexander Vogel, Jess Li, Yifei Li, Luke A. Clifton, Sebastian Daum, Kirsten Bacia, Daniel Huster, Paul A. Randazzo, Mathias Lösche, Emad Tajkhorshid, R. Andrew Byrd
Format: Article
Language:English
Published: Nature Portfolio 2023-11-01
Online Access:https://doi.org/10.1038/s41467-023-43008-5