IQGAP1 mediates the structure and dynamics of a novel multi-vesicular compartment

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dc.contributor.advisorDiehl, Michael Ren_US
dc.creatorSamson, Edward Ben_US
dc.date.accessioned2017-07-31T16:23:25Zen_US
dc.date.available2017-07-31T16:23:25Zen_US
dc.date.created2016-12en_US
dc.date.issued2016-08-08en_US
dc.date.submittedDecember 2016en_US
dc.date.updated2017-07-31T16:23:26Zen_US
dc.description.abstractIQGAP1 is a master cytoskeletal regulatory protein that connects extracellular signaling to changes in cell polarity, motility, and adhesion with adjacent cells. IQGAP1 achieves these fundamental outcomes by acting as a scaffolding protein that coordinates a wide variety of signaling cascades in a highly spatially-dependent manner. This dissertation details the use of multiple imaging modalities to characterize localized, highly-dynamic IQGAP1-related processes in epithelial MCF-10A cells. This led to the discovery of a novel multi-vesicular compartment that is surrounded by an outer layer of IQGAP1-associated actin filaments. Further studies showed that this compartment shares many common identifiers with traditional multi-vesicular bodies and participates in the internalization of cell-cell adhesion proteins via endocytic and recycling pathways. Live-cell imaging studies were conducted to correlate local cytoskeletal remodeling of this outer layer to various dynamic behaviors of the multi-vesicular core. These studies showed that IQGAP1 localization negatively correlates with actin polymerization during compartment formation and stabilization. During this time, rapid actin assembly appears to be constrained by a negative feedback mechanism. In contrast, IQGAP1 dissociation from the compartment’s surface is followed by a rapid, non-linear increase in actin polymerization that coincides with compartment disassembly and the release of multiple, high-motile intraluminal vesicles. Taken together, these results suggest a potential regulatory role of IQGAP1 in the trafficking of cell-cell adhesion proteins by promoting the stabilization of a novel multi-vesicular sorting compartment.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationSamson, Edward B. "IQGAP1 mediates the structure and dynamics of a novel multi-vesicular compartment." (2016) Diss., Rice University. <a href="https://hdl.handle.net/1911/95575">https://hdl.handle.net/1911/95575</a>.en_US
dc.identifier.urihttps://hdl.handle.net/1911/95575en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectIQGAP1en_US
dc.subjectactinen_US
dc.subjectmembraneen_US
dc.subjectdynamicsen_US
dc.subjectcell-cell adhesionen_US
dc.subjectadherens junctionsen_US
dc.subjectepithelialen_US
dc.subjectSTORMen_US
dc.titleIQGAP1 mediates the structure and dynamics of a novel multi-vesicular compartmenten_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentBioengineeringen_US
thesis.degree.disciplineEngineeringen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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