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Richard A Cerione

Goldwin Smith Professor

Research Focus

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.

Educational Background

  • PhD, Rutgers College, 1979
  • BS, Rutgers College, 1973

Research Grants

  • MACROMOLECULAR DIFFRACTION RESOURCE: MACCHESS
  • BIOCHEMICAL CHARACTERIZATION OF SIGNAL TRANSDUCTION
  • EXAMINING A NOVEL LINK BETWEEN RHO GTPASES AND THE METABOLIC MACHINERY OF HUMAN BREAST CANCER CELLS
  • ROLE OF GTP-BINDING/TRANSGLUTAMINASE IN CELL SURVIVAL
  • BIOCHEMICAL REGULATION OF THE RAS-LIKE PROTEIN, CDC42
  • ROLES OF CDC42 AND ITS SIGNALING PARTNERS IN CELL GROWTH AND DIFFERENTIATION
  • MACROM0LECULAR DIFFRACTION RESOURCE: MACCHESS
  • CHARACTERIZATION OF GROWTH FACTOR-COUPLED SIGNALING
  • ROLE OF GTP-BINDING/TRANSGLUTAMINASE IN CELL SURVIVAL AND MIGRATION

Selected Publications

PubMed Listings
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.

Wu, W.J; Erickson, J.W.; Cerione, R.A. The subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000, 405, 800.

Hoffman, G.R.; Cerione, R.A. Rac inserts its way into the immune response. Nature Immunology 2001, 2, 194.

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.