Abstract
The BIN-Amphiphysin-Rvs (BAR) domain is an evolutionarily conserved region found in over 750 proteins. BAR domain superfamily members dimerize to form a surface capable of membrane sensing and binding. Such membrane remodeling is essential for the organization and function of intracellular organelles, thus influencing important cellular events, including endocytic and membrane trafficking, cell cycle, division, and migration. In this article, we examine the different subfamilies of BAR domain proteins and discuss how they exert their influence to shape membranes. We also focus on the roles of key BAR domain proteins and their roles in mediating actin assembly and intracellular transport and signaling.
Original language | English (US) |
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Title of host publication | Encyclopedia of Cell Biology |
Subtitle of host publication | Volume 1-6, Second Edition |
Publisher | Elsevier |
Pages | 657-671 |
Number of pages | 15 |
Volume | 2 |
ISBN (Electronic) | 9780128216248 |
DOIs | |
State | Published - Jan 1 2022 |
Keywords
- BAR domain
- Clathrin-coated pits
- Curvature-sensing
- Cytoskeleton
- Dimerization
- Dynamin
- Membrane curvature
- Nucleation promoting factors
- PHOX-domain and Pleckstrin homology domain
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology