Areas of Interest
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.
Selected 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 α-tubulin mutation affects astral
microtubules and nuclear positioning during anaphase in
Saccharomyces cerevisiae: Possible role for palmitoylation of α-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 signaling. J. Biol. Chem. 274 (26): 18836-18842. |
