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

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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)61-69.e3
JournalStructure
Volume29
Issue number1
DOIs
StatePublished - Jan 7 2021

Bibliographical note

Funding Information:
We thank Drs. Andrew Kehr and Hong-Gang Wang for generously gifting us HRV-3C protease and endophilin B1 plasmids. This work was funded by The Hormel Foundation and the Paint the Town Pink Foundation for Breast Cancer Research .

Keywords

  • BAR proteins
  • amphipathic helices
  • auto-inhibition
  • membrane remodeling

PubMed: MeSH publication types

  • Journal Article

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