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Boomerangs, Bananas and Blimps: Structure and Function of F‑BAR Domains in the Context of the BAR Domain Superfamily

This chapter appears in the following book:

The Pombe Cdc15 Homology Proteins

Edited by: Pontus Aspenström
ISBN: TBA
» Get more information about this book at landesbioscience.com «

Chapter authors:
Adam Frost, Vinzenz M. Unger and Pietro De Camilli


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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 superfamily, a subset of 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 of the BAR domain superfamily and discuss the proposed mechanisms underlying their membrane‑molding activity and regulation. We end by highlighting the functional properties of select F‑BAR domains that were elucidated by electron cryo‑microscopy and 3D reconstruction of these modules while bound to flat and curved membranes.

Adam Frost
Departments of Molecular Biophysics and Biochemistry and Interdepartmental Neuroscience Program, Yale University School of Medicine

Vinzenz M. Unger
Departments of Molecular Biophysics and Biochemistry and Interdepartmental Neuroscience Program, Yale University School of Medicine

Pietro De Camilli
Departments of Molecular Biophysics, Biochemistry and Cell Biology, Interdepartmental Neuroscience Program, Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University School of Medicine

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