A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature, Developmental Cell，Available online 2 October 2014
发布时间：2014年10月13日
Developmental Cell, Available online 2 October 2014, DOI: 10.1016/j.devcel.2014.08.020
A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature
Xiaoyun Pang1, 2, Jun Fan3, Yan Zhang1, Kai Zhang1, Bingquan Gao1, 2, Jun Ma1, 2, Jian Li4, 5, Yuchen Deng1, 2, Qiangjun Zhou1, 8, Edward H. Egelman7, Victor W. Hsu4, 5, Fei Sun1, 6
Summary
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.
附件下载：
A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature, Developmental Cell，Available online 2 October 2014
Developmental Cell, Available online 2 October 2014, DOI: 10.1016/j.devcel.2014.08.020
A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature
Xiaoyun Pang1, 2, Jun Fan3, Yan Zhang1, Kai Zhang1, Bingquan Gao1, 2, Jun Ma1, 2, Jian Li4, 5, Yuchen Deng1, 2, Qiangjun Zhou1, 8, Edward H. Egelman7, Victor W. Hsu4, 5, Fei Sun1, 6
Summary
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.
相关报道：http://www.ibp.cas.cn/kyjz/zxdt/201410/t20141013_4222656.html
文章链接：http://www.cell.com/developmental-cell/abstract/S1534-5807(14)00550-4