| 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. |
