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Full-Text Articles in Cell Biology

Analysis Of Two Centrin-Binding Proteins, Poc5 And Sfr1, In Tetrahymena Thermophila Basal Bodies, Westley Heydeck Jan 2016

Analysis Of Two Centrin-Binding Proteins, Poc5 And Sfr1, In Tetrahymena Thermophila Basal Bodies, Westley Heydeck

Molecular, Cellular, and Developmental Biology Graduate Theses & Dissertations

Basal bodies are microtubule-based structures which template, anchor, and orient cilia at the cell surface. Although basal bodies contribute to vital cell functions, the molecular contributors of their assembly and maintenance are poorly understood. Previous studies in Tetrahymena thermophila revealed important roles for centrins in basal body assembly, separation of new basal bodies, and stability. Here, I characterized the basal body function of two centrin-binding proteins, Sfr1 and Poc5, in Tetrahymena. Sfr1 is the only centrin-binding protein in Tetrahymena that localizes to all cortical row and oral apparatus basal bodies. Poc5, on the other hand, transiently localizes to basal bodies ...


Polyomavirus Interactions With Host Cell Surface Receptors Mediate Important Steps In Virus Infection: From Signaling To Pathogenesis, Samantha D. O'Hara Jan 2016

Polyomavirus Interactions With Host Cell Surface Receptors Mediate Important Steps In Virus Infection: From Signaling To Pathogenesis, Samantha D. O'Hara

Molecular, Cellular, and Developmental Biology Graduate Theses & Dissertations

Virus binding to the cell surface triggers an array of host responses important for infection. Gangliosides are the cell surface receptors for Polyomavirus (PyV) infection. Specificity is determined by recognition of carbohydrate moieties on the ganglioside by the major viral capsid protein VP1 and alterations in ganglioside binding cause dramatic changes in virus tropism and pathogenesis. Knockout mice lacking complex gangliosides are completely resistant to Mouse Polyomavirus (MuPyV) infection. Fibroblasts (MEFs) from these mice are likewise resistant to infection, and supplementation with specific gangliosides: GD1a, GT1b, and GT1a rescues infection. MuPyV also binds a protein receptor α4-integrin and loss of ...


Investigating The Molecular Mechanisms And Functions Of The Musashi-2 Rna-Binding Protein, Christopher Bennett Jan 2016

Investigating The Molecular Mechanisms And Functions Of The Musashi-2 Rna-Binding Protein, Christopher Bennett

Molecular, Cellular, and Developmental Biology Graduate Theses & Dissertations

The Musashi (Msi) family of RNA-binding proteins is post-transcriptional regulators of gene expression. They were discovered in 1994 as being required for Drosophila sensory organ development. Since then, Msi proteins have been found to enhance cell proliferation and maintain stem cell identities in a multitude of mammalian tissues. In addition, overexpression of Msi proteins is often observed in many types of human cancers, most prominently the widely expressed Msi family member, Musashi-2 (Msi2). Msi2 plays oncogenic roles in hematopoietic, neural, and gastrointestinal tissues. However, Msi2 has received little attention in other tissues in which it is expressed, such as in ...


Activation And Utilization Of Dna Damage Signaling By Murine Polyomavirus, Katie Heiser Jan 2016

Activation And Utilization Of Dna Damage Signaling By Murine Polyomavirus, Katie Heiser

Molecular, Cellular, and Developmental Biology Graduate Theses & Dissertations

Nuclear replication of DNA viruses activates DNA damage repair (DDR) pathways, which may detect and inhibit viral replication. However, many DNA viruses also depend on these pathways in order to optimally replicate their genomes. I investigated the relationship between murine polyomavirus (MuPyV) and components of DDR signaling pathways including CHK1, CHK2, H2AX, ATR, ATM, RPA, MRN, and DNAPK. I found that recruitment and retention of DDR proteins at viral replication centers was independent of H2AX, as well as the viral small and middle T-antigens. Additionally, infectious virus production required ATR kinase activity, but was independent of CHK1, CHK2, or DNAPK ...