https://scholars.lib.ntu.edu.tw/handle/123456789/573365
標題: | ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages | 作者: | Chan C JIA-WEI HSU et al. |
關鍵字: | membrane protein; protein ACAP1; unclassified drug; ACAP1 protein, human; guanosine triphosphatase activating protein; membrane protein; arfgap with coil coil ankryin repeat and pleckstrin homology domain I; guanosine triphosphatase activating protein; Article; cryoelectron sub tomography; dimerization; electron microscopy; electron tomography; membrane deformation; membrane structure; molecular dynamics; Monte Carlo method; protein assembly; protein structure; protein transport; cell membrane; chemistry; human; metabolism; pleckstrin homology domain; protein conformation; controlled study; phenomena and functions of biological membrane; simulation; Cell Membrane; Dimerization; GTPase-Activating Proteins; Humans; Membrane Proteins; Pleckstrin Homology Domains; Protein Conformation | 公開日期: | 2019 | 卷: | 15 | 期: | 7 | 來源出版物: | PLoS Computational Biology | 摘要: | Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) into an unusual lattice structure that also uncovers a new paradigm for how a BAR protein deforms membrane. Here, we initially pursued computation-based refinement of the ACAP1 lattice to identify its critical protein contacts. Simulation studies then revealed how ACAP1, which dimerizes into a symmetrical structure in solution, is recruited asymmetrically to the membrane through dynamic behavior. We also pursued electron microscopy (EM)-based structural studies, which shed further insight into the dynamic nature of the ACAP1 lattice assembly. As ACAP1 is an unconventional BAR protein, our findings broaden the understanding of the mechanistic spectrum by which proteins assemble into higher-ordered structures to achieve membrane deformation. ? 2019 Chan et al. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85070788968&doi=10.1371%2fjournal.pcbi.1007081&partnerID=40&md5=c9a21115642251fb24ab6efe3f173592 https://scholars.lib.ntu.edu.tw/handle/123456789/573365 |
ISSN: | 1553734X | DOI: | 10.1371/journal.pcbi.1007081 |
顯示於: | 生化科學研究所 |
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