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

doi:10.1201/9781498712798-7

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 proceeding › Chapter

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 language	English (US)
Title of host publication	The Pombe Cdc15 Homology Proteins
Publisher	CRC Press
Pages	1-10
Number of pages	10
ISBN (Electronic)	9781498712798
ISBN (Print)	9781587063138
DOIs	https://doi.org/10.1201/9781498712798-7
State	Published - Jan 1 2009
Externally published	Yes

ASJC Scopus subject areas

General Agricultural and Biological Sciences
General Biochemistry, Genetics and Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1201/9781498712798-7

Cite this

@inbook{03912cdc96ea4419ab4c43bdc8260f41,

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

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.",

author = "Adam Frost and Unger, {Vinzenz M.} and {De Camilli}, Pietro",

note = "Publisher Copyright: {\textcopyright} 2009 by Taylor and Francis Group, LLC.",

year = "2009",

month = jan,

day = "1",

doi = "10.1201/9781498712798-7",

language = "English (US)",

isbn = "9781587063138",

pages = "1--10",

booktitle = "The Pombe Cdc15 Homology Proteins",

publisher = "CRC Press",

}

TY - CHAP

T1 - Boomerangs, bananas and blimps

T2 - Structure and function of F-BAR domains in the context of the BAR domain superfamily

AU - Frost, Adam

AU - Unger, Vinzenz M.

AU - De Camilli, Pietro

PY - 2009/1/1

Y1 - 2009/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85075311077&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85075311077&partnerID=8YFLogxK

U2 - 10.1201/9781498712798-7

DO - 10.1201/9781498712798-7

M3 - Chapter

AN - SCOPUS:85075311077

SN - 9781587063138

SP - 1

EP - 10

BT - The Pombe Cdc15 Homology Proteins

PB - CRC Press

ER -

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

Abstract

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this