Joan M. Caron
Assistant Professor
Department of Cell Biology
University of Connecticut Health Center
263 Farmington Ave
Farmington, CT 06032
860 679 2845
860 679 1269 (fax)
caron@nso1.uchc.edu
Research interests:
Dr. Caron has discovered that tubulin, the major protein of microtubules, is post-translationally modified by palmitoylation. Palmitoylation is the covalent attachment of the long chain fatty acid, palmitate, to cysteine residues of proteins. This modification has been found to regulate signaling events from the cell surface, including those involved in cell proliferation and apoptosis. Palmitoylation of tubulin, which is reversible, appears to lead to an interaction between microtubules and the plasma membrane. Our primary goal now is to determine how this interaction affects cellular functions. In addition, chemotherapeutic drugs used against cancer prevent the palmitoylation of tubulin, suggesting that palmitoylation of tubulin may be a new, more specific target for chemotherapeutic agents. To achieve this goal, we are using biochemical, cell biological and genetic approaches with both mammalian cells and the yeast Saccharomyces cerevisiae.
Recent publications
Caron, JM, and Herwood, M. The Chemotherapeutic Drug Vinblastine, Inhibits Palmitoylation of Tubulin in Human Leukemic Lymphocytes. Chemotherapy In Press
Hiol, A., Caron, J.M., and Jones, T.L.Z (2003) Purification and characterization of protein acyl transferase activity from rat liver. Biochim. Biophys. Acta 1635: 10-19.
Caron, J.M., Vega, L., Fleming, J., Bishop, Robert, and Solomon, F. (2000) Single site
a-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of a-tubulin. Mol. Biol. Cell 12: 2672-2687.
Druey, K.M., Ugur,O., Caron, J.M., Chen, C.K., Backlund, P.S., and Jones, T.L.Z. (1999) Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq signalling. J. Biol. Chem. 274 (26): 18836-18842
