Assembly of curvature-coupled proteins on deformable membranes /

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Bibliographic Details
Author / Creator:Simunovic, Mijo, author.
Imprint:2015.
Ann Arbor : ProQuest Dissertations & Theses, 2015
Description:1 electronic resource (196 pages)
Language:English
Format: E-Resource Dissertations
Local Note:School code: 0330
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/10773088
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Other authors / contributors:University of Chicago. degree granting institution.
ISBN:9781321883398
Notes:Advisors: Gregory A. Voth Committee members: Ka Yee Lee; Suri Vaikuntanathan.
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Dissertation Abstracts International, Volume: 76-11(E), Section: B.
English
Summary:Many biological phenomena are accompanied by the change in shape of the cell membrane. This process is often mediated by curvature-generating proteins, most notably by those containing one of many BAR domains. At the same time, membrane curvature controls the way proteins interact with one another and so it acts as a vital signaling mechanism in the cell. In our work, presented in two theses, we combine theoretical modeling, high-resolution imaging, and quantitative microscopy techniques to study the assembly of BAR proteins on the membrane and its influence on membrane shape and mechanics. Our simulations elucidate the molecular mechanism underlying the self-assembly of BAR proteins on the membrane and the way their collective behavior affects the large-scale membrane reshaping. Experimental biophysical methods demonstrate a novel mechanism of membrane fission mediated by BAR proteins and molecular motors. It also quantifies how the formation of protein scaffolds alters the mechanical behavior of the membrane. Our combined theoretical and experimental approach gives vital clues on how the mechanical properties of the membrane may regulate protein dynamics in living cells.