論文

査読有り 国際誌
2018年4月17日

Membrane re-modelling by BAR domain superfamily proteins via molecular and non-molecular factors.

Biochemical Society transactions
  • Tamako Nishimura
  • ,
  • Nobuhiro Morone
  • ,
  • Shiro Suetsugu

46
2
開始ページ
379
終了ページ
389
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1042/BST20170322

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.

リンク情報
DOI
https://doi.org/10.1042/BST20170322
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29540508
URL
http://www.scopus.com/inward/record.url?eid=2-s2.0-85046907111&partnerID=MN8TOARS
URL
http://orcid.org/0000-0002-4612-0628
ID情報
  • DOI : 10.1042/BST20170322
  • ISSN : 0300-5127
  • ORCIDのPut Code : 61975506
  • PubMed ID : 29540508
  • SCOPUS ID : 85046907111

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