Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/142021
Title: | ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages | Authors: | Chan, Chun Pang, Xiaoyun Zhang, Yan Niu, Tongxin Yang, Shengjiang Zhao, Daohui Li, Jian Lu, Lanyuan Hsu, Victor W. Zhou, Jian Sun, Fei Fan, Jun |
Keywords: | Science::Biological sciences | Issue Date: | 2019 | Source: | Chan, C., Pang, X., Zhang, Y., Niu, T., Yang, S., Zhao, D., . . . Fan, J. (2019). ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages. PLoS Computational Biology, 15(7), e1007081-. doi:10.1371/journal.pcbi.1007081 | Journal: | PLoS Computational Biology | Abstract: | 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. | URI: | https://hdl.handle.net/10356/142021 | ISSN: | 1553-734X | DOI: | 10.1371/journal.pcbi.1007081 | Schools: | School of Biological Sciences | Rights: | © 2019 Chan et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | Fulltext Permission: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | SBS Journal Articles |
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