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

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dc.contributor.advisorDiehl, Michael R
dc.creatorSamson, Edward B
dc.date.accessioned2017-07-31T16:23:25Z
dc.date.available2017-07-31T16:23:25Z
dc.date.created2016-12
dc.date.issued2016-08-08
dc.date.submittedDecember 2016
dc.date.updated2017-07-31T16:23:26Z
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.
dc.format.mimetypeapplication/pdf
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>.
dc.identifier.urihttps://hdl.handle.net/1911/95575
dc.language.isoeng
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.
dc.subjectIQGAP1
dc.subjectactin
dc.subjectmembrane
dc.subjectdynamics
dc.subjectcell-cell adhesion
dc.subjectadherens junctions
dc.subjectepithelial
dc.subjectSTORM
dc.titleIQGAP1 mediates the structure and dynamics of a novel multi-vesicular compartment
dc.typeThesis
dc.type.materialText
thesis.degree.departmentBioengineering
thesis.degree.disciplineEngineering
thesis.degree.grantorRice University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy
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