Effects of CaM KII and MAP Kinase on Tubulin and Actin
Bhutta, Shujera; Ciraola, Danielle; Koeneman, Brian; and Capco, David
School of Life Sciences, Arizona State University
Investigation into the cell cycle provides information on disease and development. Localization of MAP Kinase (Mitogen Activated Protein Kinase), pPKC (Phospho Protein Kinase C) and CaM KII (Calcium/Calmodulin Dependent Protein Kinase II) was observed by using immunocytochemistry and detergent extraction techniques. Immunocytochemistry is a lab technique, which utilizes the antibodies which attach antigenic receptors on the cell cytoskeleton. Localization of MAP Kinase and CaM KII on cytoskeletal elements, tubulin and actin, develop different functions of kinases during the cell cycle. In this study we examined the state of activity and localization of CaM KII and MAP Kinase in the eukaryotic cells. It was found that tCaM KII (Phosphorylated and Non-phosphorylated forms of CaM KII) involvement was perceptible at the periphery during transition from anaphase to telophase. During telophase, tCaM kinaseII interacts with actin, which is found at the borders of cell membrane. For the duration of interphase, tCaM KII was localized in the cytoplasm, suggesting that tCaM KII has decreased interaction with actin. Phosphorylated CaM KII (pCaM KII) follows the same format as tCaM KII. Localization of pPKC was noticed at the mitotic spindle to stabilize spindle poles. Total Protein Kinase C (tPKC) was found everywhere but, pPKC was exclusively at the spindle poles. Furthermore, tMAP Kinase concentration was higher around the nucleus during interphase of the cell cycle, signifying that tMAP Kinase is interacting with tubulin