Self-assembly of filopodia-like structures on supported lipid bilayers

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 2010.

গ্রন্থ-পঞ্জীর বিবরন
প্রধান লেখক: Lee, Kwonmoo
অন্যান্য লেখক: Marc W. Kirschner.
বিন্যাস: গবেষণাপত্র
ভাষা:eng
প্রকাশিত: Massachusetts Institute of Technology 2011
বিষয়গুলি:
অনলাইন ব্যবহার করুন:http://hdl.handle.net/1721.1/62648
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author Lee, Kwonmoo
author2 Marc W. Kirschner.
author_facet Marc W. Kirschner.
Lee, Kwonmoo
author_sort Lee, Kwonmoo
collection MIT
description Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 2010.
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spelling mit-1721.1/626482019-04-12T09:38:12Z Self-assembly of filopodia-like structures on supported lipid bilayers Self-assembly of FLSs on supported lipid bilayers Lee, Kwonmoo Marc W. Kirschner. Massachusetts Institute of Technology. Dept. of Physics. Massachusetts Institute of Technology. Dept. of Physics. Physics. Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 2010. Cataloged from PDF version of thesis. Includes bibliographical references (p. 98-121). Filopodia are finger-like protrusive structures of cells, comprised of actin bundles, which can serve as sensory organelles. To probe their pathway of assembly we have reconstituted filopodia-like structures (FLSs) by applying frog egg extracts to supported lipid bilayers containing phosphatidylinositol(4,5)bisphosphate, PI(4,5)P 2. The FLSs recapitulate important characteristics of filopodia - they assemble parallel actin bundles from the lipid membrane and they form in the presence of capping activity. Known filopodial tip components such as Diaphanous-related formin and VASP localize to the membrane base of the structures, and bundling protein fascin to the shaft. Actin subunits assemble at the tip and translocate into the shaft. FLS assembly requires negativelycharged lipid membranes, with specific requirements for PI(4,5)P 2 and, for maximal efficiency, phosphatidyl-serine. The focal nature of FLSs is not a result of templating by PI(4,5)P2 microdomains but instead by the self-organization of tip complex assembly on uniform PI(4,5)P 2-enriched regions. BAR domain protein toca-1 recruits N-WASP then the Arp2/3 complex and actin assembly follow. Elongation proteins Diaphanous-related formin, VASP and fascin are recruited later. The Arp2/3 complex is absolutely required for FLS initiation but is not required for elongation, which may involve multiple factors including formins. We propose a model for filopodia formation involving an initial clustering of Arp 2/3 complex regulators, self-assembly of filopodial tip complexes on the membrane, resulting in the outgrowth of parallel actin bundles. by Kwonmoo Lee. Ph.D. 2011-05-09T15:14:01Z 2011-05-09T15:14:01Z 2010 2010 Thesis http://hdl.handle.net/1721.1/62648 713648004 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 121 p. application/pdf Massachusetts Institute of Technology
spellingShingle Physics.
Lee, Kwonmoo
Self-assembly of filopodia-like structures on supported lipid bilayers
title Self-assembly of filopodia-like structures on supported lipid bilayers
title_full Self-assembly of filopodia-like structures on supported lipid bilayers
title_fullStr Self-assembly of filopodia-like structures on supported lipid bilayers
title_full_unstemmed Self-assembly of filopodia-like structures on supported lipid bilayers
title_short Self-assembly of filopodia-like structures on supported lipid bilayers
title_sort self assembly of filopodia like structures on supported lipid bilayers
topic Physics.
url http://hdl.handle.net/1721.1/62648
work_keys_str_mv AT leekwonmoo selfassemblyoffilopodialikestructuresonsupportedlipidbilayers
AT leekwonmoo selfassemblyofflssonsupportedlipidbilayers