The Cerione group is studying signaling pathways that are important in various biological outcomes, with particular emphasis on cancer progression and neurogenesis. They are using a combination of biochemical, structural, genetic, and small molecule chemistry to probe these pathways.
Signal Transduction Mechanisms
The research efforts of my laboratory have focused on understanding the molecular mechanisms by which signals are transmitted from cell surface receptors to biological effectors. In particular, we have been interested in identifying new signaling molecules that influence the growth and differentiation of mammalian cells. Three areas of research are currently being pursued in the laboratory.
The first involves studies of the regulation and structural characterization of a cell-division-cycle, Ras-related GTP-binding protein, Cdc42. This GTP-binding protein and its regulators appear to play critical roles in cell growth, the establishment of cell polarity, and cytokinesis. In these studies, we are using a variety of biochemical, molecular biology-based, and structural techniques to obtain new insights into how this Ras-like protein, through interactions with a variety of cellular targets, can coordinate cytoskeletal changes with cell cycle progression and cell division.
A second area of research interest focuses on the structure-function comparisons of heterotrimeric G proteins and Ras-like GTP-binding proteins, where we have used the retinal G protein, transducin, as a model for developing novel fluorescence approaches to study G protein activation and G protein-target interactions. The third area of interest concerns the identification and structure-function characterization of novel GTP-binding activities present in the nucleus and engaged in regulating RNA metabolism and/or cell cycle progression.
Hoffman, G.R.; Rahl, P.B.; Collins, R.N.; Cerione, R.A. Conserved structural motifs in intracellular trafficking pathways: Structure of the gCOP appendage domain. Molecular Cell 2003, 12, 615.
Wu, W.J; Tu, S.; Cerione, R.A. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 2003, 114, 715.
Calero, G; Wilson, K.F.; Li, T.; Clardy, J.C.; Cerione, R.A. Structural basis of m7GpppG binding to the nuclear cap-binding protein complex. Nature Structural Biology 2002, 9, 912.
Hoffman, G.R.; Cerione, R.A. Rac inserts its way into the immune response. Nature Immunology 2001, 2, 194.
Wu, W.J; Erickson, J.W.; Cerione, R.A. The subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000, 405, 800.
Awards and Distinctions
- PEW Biomedical Research Scholar
- Reviewer of Laboratory of Molecular Biology, National Cancer Institute
- Eppley Institute Distinguished Lecturer in Cancer Research
- Frontiers Lecturer at Case Western Medical School