Abstract
The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 Å, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
| Original language | English |
|---|---|
| Pages (from-to) | 2889-2897 |
| Number of pages | 9 |
| Journal | EMBO Journal |
| Volume | 25 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2006 Jun 21 |
| Externally published | Yes |
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Keywords
- BAR domain
- Endophilin
- Liposome
- Membrane curvature
- Membrane insertion
ASJC Scopus subject areas
- Genetics
- Cell Biology
Cite this
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. / Masuda, Michitaka; Takeda, Soichi; Sone, Manami; Ohki, Takashi; Mori, Hidezo; Kamioka, Yuji; Mochizuki, Naoki.
In: EMBO Journal, Vol. 25, No. 12, 21.06.2006, p. 2889-2897.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
AU - Masuda, Michitaka
AU - Takeda, Soichi
AU - Sone, Manami
AU - Ohki, Takashi
AU - Mori, Hidezo
AU - Kamioka, Yuji
AU - Mochizuki, Naoki
PY - 2006/6/21
Y1 - 2006/6/21
N2 - The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 Å, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
AB - The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 Å, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
KW - BAR domain
KW - Endophilin
KW - Liposome
KW - Membrane curvature
KW - Membrane insertion
UR - http://www.scopus.com/inward/record.url?scp=33745559393&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33745559393&partnerID=8YFLogxK
U2 - 10.1038/sj.emboj.7601176
DO - 10.1038/sj.emboj.7601176
M3 - Article
C2 - 16763557
AN - SCOPUS:33745559393
VL - 25
SP - 2889
EP - 2897
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 12
ER -