 |
PDBsum entry 4ckg
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
4ckg
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
A ph domain in acap1 possesses key features of the bar domain in promoting membrane curvature.
|
|
|
Authors
|
|
X.Pang,
J.Fan,
Y.Zhang,
K.Zhang,
B.Gao,
J.Ma,
J.Li,
Y.Deng,
Q.Zhou,
E.H.Egelman,
V.W.Hsu,
F.Sun.
|
|
|
Ref.
|
|
Dev Cell, 2014,
31,
73-86.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The BAR (Bin-Amphiphysin-Rvs) domain undergoes dimerization to produce a curved
protein structure, which superimposes onto membrane through electrostatic
interactions to sense and impart membrane curvature. In some cases, a BAR domain
also possesses an amphipathic helix that inserts into the membrane to induce
curvature. ACAP1 (Arfgap with Coil coil, Ankyrin repeat, and PH domain protein
1) contains a BAR domain. Here, we show that this BAR domain can neither bind
membrane nor impart curvature, but instead requires a neighboring PH (Pleckstrin
Homology) domain to achieve these functions. Specific residues within the PH
domain are responsible for both membrane binding and curvature generation. The
BAR domain adjacent to the PH domain instead interacts with the BAR domains of
neighboring ACAP1 proteins to enable clustering at the membrane. Thus, we have
uncovered the molecular basis for an unexpected and unconventional collaboration
between PH and BAR domains in membrane bending.
|
|
|
|
|
|
|
