Boomerangs, bananas and blimps: Structure and function of F-BAR domains in the context of the BAR domain superfamily

Adam Frost, Vinzenz M. Unger*, Pietro De Camilli

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

Abstract

Proteins that belong to the BAR (Bin, Amphiphysin, RVS) domain superfamily are alpha-helical bilayer-binding modules that have evolved to induce or stabilize membrane curvature during cellular events like endocytosis, cell division and organelle biogenesis. Within the superfam­ ily, a subset o f proteins possessing F-BAR (Fes/CIP4 homology-BAR) domains play key roles in membrane remodeling and loss-of-function mutations in genes coding for F-BAR proteins are associated with human diseases. Here, we review how F-BAR domains compare structurally with related members o f the BAR domain superfamily and discuss the proposed mechanisms underlying their membrane-molding activity and regulation. We end by highlighting the functional properties o f select F-BAR domains that were elucidated by electron cryo-microscopy and 3D reconstruction o f these modules while bound to flat and curved membranes.

Original languageEnglish (US)
Title of host publicationThe Pombe Cdc15 Homology Proteins
PublisherCRC Press
Pages1-10
Number of pages10
ISBN (Electronic)9781498712798
ISBN (Print)9781587063138
DOIs
StatePublished - Jan 1 2009
Externally publishedYes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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