A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

Vikram Kjøller Bhatia; Nikos Hatzakis; Dimitrios Stamou

doi:10.1016/j.semcdb.2009.12.004

A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

Vikram Kjøller Bhatia, Nikos Hatzakis, Dimitrios Stamou

73 Citations (Scopus)

Abstract

The discovery of proteins that recognize membrane curvature created a paradigm shift by suggesting that membrane shape may act as a cue for protein localization that is independent of lipid or protein composition. Here we review recent data on membrane curvature sensing by three structurally unrelated motifs: BAR domains, amphipathic helices and membrane-anchored proteins. We discuss the conclusion that the curvature of the BAR dimer is not responsible for sensing and that the sensing properties of all three motifs can be rationalized by the physicochemical properties of the curved membrane itself. We thus anticipate that membrane curvature will promote the redistribution of proteins that are anchored in membranes through any type of hydrophobic moiety, a thesis that broadens tremendously the implications of membrane curvature for protein sorting, trafficking and signaling in cell biology.

Original language	English
Journal	Seminars in Cell and Developmental Biology
Volume	21
Issue number	4
Pages (from-to)	381-390
Number of pages	10
ISSN	1084-9521
DOIs	https://doi.org/10.1016/j.semcdb.2009.12.004
Publication status	Published - Jun 2010

Access to Document

10.1016/j.semcdb.2009.12.004

Cite this

@article{5eeed6214cc042818832194f126b984f,

title = "A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins",

abstract = "The discovery of proteins that recognize membrane curvature created a paradigm shift by suggesting that membrane shape may act as a cue for protein localization that is independent of lipid or protein composition. Here we review recent data on membrane curvature sensing by three structurally unrelated motifs: BAR domains, amphipathic helices and membrane-anchored proteins. We discuss the conclusion that the curvature of the BAR dimer is not responsible for sensing and that the sensing properties of all three motifs can be rationalized by the physicochemical properties of the curved membrane itself. We thus anticipate that membrane curvature will promote the redistribution of proteins that are anchored in membranes through any type of hydrophobic moiety, a thesis that broadens tremendously the implications of membrane curvature for protein sorting, trafficking and signaling in cell biology.",

author = "Bhatia, {Vikram Kj{\o}ller} and Nikos Hatzakis and Dimitrios Stamou",

year = "2010",

month = jun,

doi = "10.1016/j.semcdb.2009.12.004",

language = "English",

volume = "21",

pages = "381--390",

journal = "Seminars in Cell and Developmental Biology",

issn = "1084-9521",

publisher = "Academic Press",

number = "4",

}

TY - JOUR

T1 - A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

AU - Bhatia, Vikram Kjøller

AU - Hatzakis, Nikos

AU - Stamou, Dimitrios

PY - 2010/6

Y1 - 2010/6

N2 - The discovery of proteins that recognize membrane curvature created a paradigm shift by suggesting that membrane shape may act as a cue for protein localization that is independent of lipid or protein composition. Here we review recent data on membrane curvature sensing by three structurally unrelated motifs: BAR domains, amphipathic helices and membrane-anchored proteins. We discuss the conclusion that the curvature of the BAR dimer is not responsible for sensing and that the sensing properties of all three motifs can be rationalized by the physicochemical properties of the curved membrane itself. We thus anticipate that membrane curvature will promote the redistribution of proteins that are anchored in membranes through any type of hydrophobic moiety, a thesis that broadens tremendously the implications of membrane curvature for protein sorting, trafficking and signaling in cell biology.

AB - The discovery of proteins that recognize membrane curvature created a paradigm shift by suggesting that membrane shape may act as a cue for protein localization that is independent of lipid or protein composition. Here we review recent data on membrane curvature sensing by three structurally unrelated motifs: BAR domains, amphipathic helices and membrane-anchored proteins. We discuss the conclusion that the curvature of the BAR dimer is not responsible for sensing and that the sensing properties of all three motifs can be rationalized by the physicochemical properties of the curved membrane itself. We thus anticipate that membrane curvature will promote the redistribution of proteins that are anchored in membranes through any type of hydrophobic moiety, a thesis that broadens tremendously the implications of membrane curvature for protein sorting, trafficking and signaling in cell biology.

U2 - 10.1016/j.semcdb.2009.12.004

DO - 10.1016/j.semcdb.2009.12.004

M3 - Journal article

C2 - 20006726

SN - 1084-9521

VL - 21

SP - 381

EP - 390

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

IS - 4

ER -

A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

Abstract

Access to Document

Fingerprint

Cite this