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Faculty
 Joan M. Caron
Assistant Professor of Cell Biology
caron@nso1.uchc.edu
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.
Dr. Caron's Departmental Web Page
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. |
