Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation


Back to previous page
Authors: Kelley, CF; Messelaar, EM; Eskin, TL; Wang, SY; Song, KK; Vishnia, K; Becalska, AN; Shupliakov, O; Hagan, MF; Danino, D; Sokolova, OS; Nicastro, D; Rodal, AA
Year: 2015
Journal: Cell Reports 13: 2597-2609   Article Link (DOI)  PubMed
Title: Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation
Abstract: F-BAR domain proteins regulate and sense membrane curvature by interacting with negatively charged phospholipids and assembling into higher-order scaffolds. However, regulatory mechanisms controlling these interactions are poorly understood. Here, we show that Drosophila Nervous Wreck (Nwk) is autoregulated by a C-terminal SH3 domain module that interacts directly with its F-BAR domain. Surprisingly, this autoregulation does not mediate a simple "on-off'' switch for membrane remodeling. Instead, the isolated Nwk F-BAR domain efficiently assembles into higher-order structures and deforms membranes only within a limited range of negative membrane charge, and autoregulation elevates this range. Thus, autoregulation could either reduce membrane binding or promote higher-order assembly, depending on local cellular membrane composition. Our findings uncover an unexpected mechanism by which lipid composition directs membrane remodeling.
Back to previous page
 

Please send suggestions for improving this publication database to sass-support@sfu.ca.
Departmental members may update their publication list.