Subcellular membrane curvature mediated by the BAR domain superfamily proteins

Shiro Suetsugu, Kiminori Toyooka, Yosuke Senju

Research output: Contribution to journalReview article

98 Citations (Scopus)

Abstract

The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily consists of proteins containing the BAR domain, the extended FCH (EFC)/FCH-BAR (F-BAR) domain, or the IRSp53-MIM homology domain (IMD)/inverse BAR (I-BAR) domain. These domains bind membranes through electrostatic interactions between the negative charges of the membranes and the positive charges on the structural surface of homo-dimeric BAR domain superfamily members. Some BAR superfamily members have membrane-penetrating insertion loops, which also contribute to the membrane binding by the proteins. The membrane-binding surface of each BAR domain superfamily member has its own unique curvature that governs or senses the curvature of the membrane for BAR-domain binding. The wide range of BAR-domain surface curvatures correlates with the various invaginations and protrusions of cells. Therefore, each BAR domain superfamily member may generate and recognize the curvature of the membrane of each subcellular structure, such as clathrin-coated pits or filopodia. The BAR domain superfamily proteins may regulate their own catalytic activity or that of their binding proteins, depending on the membrane curvature of their corresponding subcellular structures.

Original languageEnglish
Pages (from-to)340-349
Number of pages10
JournalSeminars in Cell and Developmental Biology
Volume21
Issue number4
DOIs
Publication statusPublished - Jun 2010
Externally publishedYes

Fingerprint

Membranes
Carrier Proteins
amphiphysin
Protein Domains
Clathrin
Pseudopodia
Static Electricity
Membrane Proteins
Proteins

Keywords

  • BAR
  • EFC
  • Endocytosis
  • F-BAR
  • Filopodia
  • I-BAR
  • IMD
  • Lamellipodia
  • Membrane curvature
  • Signal transduction

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

Cite this

Subcellular membrane curvature mediated by the BAR domain superfamily proteins. / Suetsugu, Shiro; Toyooka, Kiminori; Senju, Yosuke.

In: Seminars in Cell and Developmental Biology, Vol. 21, No. 4, 06.2010, p. 340-349.

Research output: Contribution to journalReview article

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