Lipid membranes are structural components of cell surfaces and intracellular organelles. Alterations in lipid membrane shape are accompanied by numerous cellular functions, including endocytosis, intracellular transport, and cell migration. Proteins containing Bin–Amphiphysin–Rvs (BAR) domains (BAR proteins) are unique, because their structures correspond to the membrane curvature, that is, the shape of the lipid membrane. BAR proteins present at high concentration determine the shape of the membrane, because BAR domain oligomers function as scaffolds that mould the membrane. BAR proteins co-operate with various molecular and non-molecular factors. The molecular factors include cytoskeletal proteins such as the regulators of actin filaments and the membrane scission protein dynamin. Lipid composition, including saturated or unsaturated fatty acid tails of phospholipids, also affects the ability of BAR proteins to mould the membrane. Non-molecular factors include the external physical forces applied to the membrane, such as tension and friction. In this mini-review, we will discuss how the BAR proteins orchestrate membrane dynamics together with various molecular and non-molecular factors.
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April 2018
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A 3D rendering of a Ubiquitin protein molecule. In this issue of Biochemical Society Transactions, Ovaa and Vertegaal discuss the role of ubiquitination and SUMO proteins in conjugation and deconjugation machineries; for details, see pages 423–436.
Review Article|
March 14 2018
Membrane re-modelling by BAR domain superfamily proteins via molecular and non-molecular factors
Tamako Nishimura;
1Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
Correspondence: Tamako Nishimura (tnishimura@bs.naist.jp) or Shiro Suetsugu (suetsugu@bs.naist.jp)
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Nobuhiro Morone;
Nobuhiro Morone
2MRC Toxicology Unit, University of Leicester, Leicester LE1 9HN, U.K.
3Institute for Integrated Cell-Material Sciences (iCeMS), Kyoto University, Kyoto 606-8501, Japan
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Shiro Suetsugu
1Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
Correspondence: Tamako Nishimura (tnishimura@bs.naist.jp) or Shiro Suetsugu (suetsugu@bs.naist.jp)
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Publisher: Portland Press Ltd
Received:
December 03 2017
Revision Received:
January 26 2018
Accepted:
January 30 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (2): 379–389.
Article history
Received:
December 03 2017
Revision Received:
January 26 2018
Accepted:
January 30 2018
Citation
Tamako Nishimura, Nobuhiro Morone, Shiro Suetsugu; Membrane re-modelling by BAR domain superfamily proteins via molecular and non-molecular factors. Biochem Soc Trans 17 April 2018; 46 (2): 379–389. doi: https://doi.org/10.1042/BST20170322
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