Office Phone: 318-675-5164
Office Fax: 318-675-5180
B.A., 1983, University of Maryland
Ph.D., 1989, University of Pennsylvania
Dr. Robinson's major research interests are control of cell growth and division, protein phosphorylation, vesicular trafficking, and yeast genetics.
Control of cell growth and division; protein phosphorylation and vesicular trafficking; yeast genetics. Protein phosphorylation is a major post-translational regulatory mechanism in eukaryotic cells. Numerous protein kinases influence diverse aspects of cell growth and division, differentiation, and environmental adaptation. The activities of protein kinases are often linked in cascades, in which activation of a kinase is itself accomplished by phosphorylation. This can result in a response system that is sensitive to multiple input signals and can adjust levels of response to varying levels of signal. Our laboratory focuses on the biological activities and regulation of yeast protein kinases (Yck=yeast casein kinase I) that is ideally suited to participate in phosphorylation cascades. Casein kinase I (CK1) proteins recognize a Ser or Thr in an acidic context and can act on substrate sites in which the acidic moiety is a phosphorylated residue. Therefore, phosphorylation by these protein kinases can be targeted by a previous phosphorylation event. Five CK1 isoforms have been identified in mammalian cells. We identified the Yck1/2 CK1 isoforms in yeast based on their combined effects on cellular responses to environmental stress. Our research is directed toward identifying the biological roles, targets, and regulation of the Yck1/2 proteins. Yck1/2 activity is essential to yeast cell viability and is required for multiple cellular pathways. Current projects concern the roles of the Yck1/2 proteins in protein trafficking and cellular morphogenesis, biologically relevant substrates, and the mechanisms of regulation of Yck2 activity. We also maintain active collaborations with the Leidenheimer and Tatchell labs.
All Publications: PubMed