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-Structure paper
タイトル | A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature. |
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ジャーナル・号・ページ | Dev Cell, Vol. 31, Issue 1, Page 73-86, Year 2014 |
掲載日 | 2014年10月13日 |
著者 | Xiaoyun Pang / Jun Fan / Yan Zhang / Kai Zhang / Bingquan Gao / Jun Ma / Jian Li / Yuchen Deng / Qiangjun Zhou / Edward H Egelman / Victor W Hsu / Fei Sun / |
PubMed 要旨 | 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 ...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. |
リンク | Dev Cell / PubMed:25284369 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 2.2 - 17.0 Å |
構造データ | EMDB-2546, PDB-4ckg: EMDB-2547, PDB-4ckh: PDB-4nsw: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | SIGNALING PROTEIN / MEMBRANE REMODELING / PROTEIN TRANSPORT / COILED-COIL / BAR DOMAIN / PH DOMAIN / GTPASE ACTIVATION |