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dc.contributor.advisor Bennett, Vann en_US
dc.contributor.author Dowless, Kayla M. en_US
dc.date.accessioned 2012-01-12T13:38:06Z
dc.date.available 2012-01-12T13:38:06Z
dc.date.issued 2011 en_US
dc.identifier.uri http://hdl.handle.net/10161/5051
dc.description Thesis en_US
dc.description.abstract <p>The ankyrin family of proteins form specialized membrane domains in various cell types, including neurons and cardiomyocytes but little is known about how this process occurs. The majority of ankyrins localize to the plasma membrane in these cells while ankyrins in fibroblasts are largely intracellular. This property of fibroblasts allows us to study intracellular ankyrin and potentially how ankyrin forms membrane domains in other cell types. In this thesis, we use western blots, immunofluorescence, RT-PCR to characterize the expression pattern of ankyrin in fibroblasts and find that both ankyrin-B and -G localize to both nuclear and intracellular compartments. The size of the compartments of both ankyrin-B and -G is affected by the genetic deletion of the large isoforms of ankyrin-B and -G. The ankyrin-B compartment has a weak association with recycling endosomes suggesting that ankyrin-B may be involved in membrane protein trafficking.</p> en_US
dc.subject Cellular biology en_US
dc.subject Ankyrin en_US
dc.subject Fibroblast en_US
dc.title Fibroblasts as a Window into the Cell Biology of Ankyrin -B and -G en_US
dc.type Thesis en_US
dc.department Cell Biology en_US

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