IntroductionProfessor Danton H. O'Day's Research
Research in Professor Danton H. O'Day's lab focuses on the roles of calmodulin binding proteins (CaMBPs) in cell function. Most of this research involves the model eukaryotic microbe Dictyostelium but collaborations with others have involved studies on Alzheimer's Disease, maternal behaviour, muscle contraction and breast cancer cell motility.
Work using the CaM-binding overlay technique (CaMBOT) has led to the isolation of many CaMBPs from Dictyostelium. A novel nuclear CaMBP called nucleomorphin, a multidomain protein that regulates nuclear number, exists in various isoforms possessing a calmodulin binding domains, nuclear localization sequences and a BRCT domain. Dictyostelium phosphoglycerate kinase and thymidine kinase were found to be very similar to the human enzymes and also to bind to and be regulated in part by CaM. A novel 46kDa CaMBP, cmbB, is primarily constructed of a 22 amino acid repeat that is also present in proteins from Mimi Virus. This research is slowly working its way towards elucidating how populations of CaMBPs work together to effect cellular and developmental processes.
Professor O'Day has studied aspects of cellular slime mould development in Dictyostelium and other species and details this work in the "Life Cycles" section. Professor O'Day's other interests include developing his teaching websites through the use of detailed graphics and animations. He has also carried out research and published articles on the value of animations in biology teaching. His hobbies include writing music, books and developing educational games as detailed on pages or links available in this website.