Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling

Veer S. Bhatt; Robert Ashley; Anna Sundborger-Lunna

doi:10.1016/j.str.2020.09.012

Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling

Veer S. Bhatt, Robert Ashley, Anna Sundborger-Lunna

Hormel Institute

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Bhatt et al. use cryo-EM to reveal the organization of N-BAR protein endophilin B1 assembled on tubulated membranes. Interactions between N-terminal amphipathic motif H0 and membrane lipids direct helical assembly of dimers. Membrane binding and subsequent remodeling is auto-inhibited, mediated by H0-SH3 domain interactions, and influenced by membrane lipid composition.

Original language	English (US)
Pages (from-to)	61-69.e3
Journal	Structure
Volume	29
Issue number	1
DOIs	https://doi.org/10.1016/j.str.2020.09.012
State	Published - Jan 7 2021

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Publisher Copyright:
© 2020 Elsevier Ltd

Keywords

BAR proteins
amphipathic helices
auto-inhibition
membrane remodeling

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Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling

Abstract

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Keywords

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