Poster Session #2
Presentation Type
Poster - Campus Access Only
Faculty Mentor’s Full Name
Ekaterina Voronina
Faculty Mentor’s Department
Division of Biological Sciences
Abstract / Artist's Statement
The regulation of RNA-binding protein (RBP) activity in cells is a central question in gene expression studies. One important RBP is GLD-1; this protein family acts as a tumor suppressor, in both mice and nematodes. Previous research from our laboratory revealed that a small protein, DLC-1, promoted the functions of GLD-1 in Caenorhabditis elegans (roundworm). Understanding this relationship between DLC-1 and GLD-1 is important for understanding stem cell balance; when the balance between mitotic proliferation and differentiation is altered, it can result in serious consequences such as tumor formation and cancer. After establishing that DLC-1 promoted GLD-1 function (Ellenbecker et al., in revision), we wondered if this interaction was conserved in mammalian cells. Mice have two DLC-1 homologues, DYNLL1 and DYNLL2, and several GLD-1 homologues including Sam68, QKI6, and QKI7. We hypothesized that there would be an interaction between some of these homologous proteins found in mice because there is an interaction between DLC-1 and GLD-1 in the worm. I tested this hypothesis by performing GST pulldown assay experiments and then doing a western blot of the samples to detect any potential interaction. After testing all pairwise combinations of DYNLL1/DYNLL2 and Sam68/QKI6/QKI7, we were able to conclude that the interaction found in the nematode was not conserved in these homologues in mice. However, there are still other mouse homologues that we have yet to test and could potentially interact. If we obtain these other homologues and identify an interaction, understanding it at a molecular level in mammalian cells would advance our understanding of certain human diseases like cancer, and potential to apply it to medical practice.
Category
Health and Medical Science
Is the protein-protein interaction discovered in the nematode conserved for mammalian proteins?
UC South Ballroom
The regulation of RNA-binding protein (RBP) activity in cells is a central question in gene expression studies. One important RBP is GLD-1; this protein family acts as a tumor suppressor, in both mice and nematodes. Previous research from our laboratory revealed that a small protein, DLC-1, promoted the functions of GLD-1 in Caenorhabditis elegans (roundworm). Understanding this relationship between DLC-1 and GLD-1 is important for understanding stem cell balance; when the balance between mitotic proliferation and differentiation is altered, it can result in serious consequences such as tumor formation and cancer. After establishing that DLC-1 promoted GLD-1 function (Ellenbecker et al., in revision), we wondered if this interaction was conserved in mammalian cells. Mice have two DLC-1 homologues, DYNLL1 and DYNLL2, and several GLD-1 homologues including Sam68, QKI6, and QKI7. We hypothesized that there would be an interaction between some of these homologous proteins found in mice because there is an interaction between DLC-1 and GLD-1 in the worm. I tested this hypothesis by performing GST pulldown assay experiments and then doing a western blot of the samples to detect any potential interaction. After testing all pairwise combinations of DYNLL1/DYNLL2 and Sam68/QKI6/QKI7, we were able to conclude that the interaction found in the nematode was not conserved in these homologues in mice. However, there are still other mouse homologues that we have yet to test and could potentially interact. If we obtain these other homologues and identify an interaction, understanding it at a molecular level in mammalian cells would advance our understanding of certain human diseases like cancer, and potential to apply it to medical practice.