Giant vesicles compressed by actin polymerization

Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Physics, 2004. === Includes bibliographical references (p. 45-46). === This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections. === Actin polymeriz...

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Main Author: Carrel, Hyman A. (Hyman Andrew), 1979-
Other Authors: Alexander van Oudenaarden.
Format: Others
Language:English
Published: Massachusetts Institute of Technology 2005
Subjects:
Online Access:http://hdl.handle.net/1721.1/16646
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spelling ndltd-MIT-oai-dspace.mit.edu-1721.1-166462019-05-02T16:17:10Z Giant vesicles compressed by actin polymerization Carrel, Hyman A. (Hyman Andrew), 1979- Alexander van Oudenaarden. Massachusetts Institute of Technology. Dept. of Physics. Massachusetts Institute of Technology. Dept. of Physics. Physics. Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Physics, 2004. Includes bibliographical references (p. 45-46). This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections. Actin polymerization plays a critical role in generating propulsive force to drive many types of cell motility. The discovery of actin based motility of the bacterial pathogen Listeria monocytogenes has lead to clearer understandings of the essential ingredients required for cell motility. The biophysical mechanisms by which these proteins generate forces is the subject of intense investigation. A novel system to study force generation by this polymerization engine is introduced by combining the well characterized mechanical properties of synthetic Giant Vesicles with the well understood biochemistry of actin polymerization. Giant Vesicles mimic the structural features of eukaryotic cell membranes. We find that Giant Vesicles coated with a protein that catalyzes actin polymerization form thick actin shells which produce a compressive force. The polymerization force directed at the membrane interface causes the membrane to rupture. In the resulting collapse we find that the shell thickens inward with a constant radial velocity and is characterized by radial lines of lipid and actin. We show that actin polymerization is the primary force driving the collapse. by Hyman A. Carrel. S.M. 2005-05-17T14:47:06Z 2005-05-17T14:47:06Z 2004 2004 Thesis http://hdl.handle.net/1721.1/16646 56219039 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 46 p. 610431 bytes 12337501 bytes application/pdf application/pdf application/pdf Massachusetts Institute of Technology
collection NDLTD
language English
format Others
sources NDLTD
topic Physics.
spellingShingle Physics.
Carrel, Hyman A. (Hyman Andrew), 1979-
Giant vesicles compressed by actin polymerization
description Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Physics, 2004. === Includes bibliographical references (p. 45-46). === This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections. === Actin polymerization plays a critical role in generating propulsive force to drive many types of cell motility. The discovery of actin based motility of the bacterial pathogen Listeria monocytogenes has lead to clearer understandings of the essential ingredients required for cell motility. The biophysical mechanisms by which these proteins generate forces is the subject of intense investigation. A novel system to study force generation by this polymerization engine is introduced by combining the well characterized mechanical properties of synthetic Giant Vesicles with the well understood biochemistry of actin polymerization. Giant Vesicles mimic the structural features of eukaryotic cell membranes. We find that Giant Vesicles coated with a protein that catalyzes actin polymerization form thick actin shells which produce a compressive force. The polymerization force directed at the membrane interface causes the membrane to rupture. In the resulting collapse we find that the shell thickens inward with a constant radial velocity and is characterized by radial lines of lipid and actin. We show that actin polymerization is the primary force driving the collapse. === by Hyman A. Carrel. === S.M.
author2 Alexander van Oudenaarden.
author_facet Alexander van Oudenaarden.
Carrel, Hyman A. (Hyman Andrew), 1979-
author Carrel, Hyman A. (Hyman Andrew), 1979-
author_sort Carrel, Hyman A. (Hyman Andrew), 1979-
title Giant vesicles compressed by actin polymerization
title_short Giant vesicles compressed by actin polymerization
title_full Giant vesicles compressed by actin polymerization
title_fullStr Giant vesicles compressed by actin polymerization
title_full_unstemmed Giant vesicles compressed by actin polymerization
title_sort giant vesicles compressed by actin polymerization
publisher Massachusetts Institute of Technology
publishDate 2005
url http://hdl.handle.net/1721.1/16646
work_keys_str_mv AT carrelhymanahymanandrew1979 giantvesiclescompressedbyactinpolymerization
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