Medical Student Research Fellowship for Summer 2003

Mentor: Sandy Hofmann
Department: Internal Medicine/Hamon Center for Therapeutic Oncology Research
Room number: NB8.104A
Mail Code: 8593
Phone number: 214-648-4911
E-mail: Sandra.Hofmann@UTSouthwestern.edu
Project title: Regulation of Protein S-Acylation and Deacylation

Human subjects IRB approved project number (where applicable):Not applicable

Animal subjects IRB approved project number (where applicable): Not applicable

Project Type (patient-based research, animal-based research, or basic research; this characterization is only to permit a general classification for grouping similar types of projects): Basic

Brief Description of Project:

My laboratory studies mechanisms involved in the covalent attachment of fatty acids to proteins. Covalent attachment of fatty acids to cysteine residues in proteins (protein S-acylation) is used by cells to mediate interactions of proteins with membranes and with each other. The fatty acid modification is reversible and the fatty acylation status of some proteins changes when they participate in signaling events. We are studying the mechanism of fatty acylation of H-Ras and N-Ras through cell culture and molecular biological techniques. The project would involve studying the acylation status of these Ras isoforms in response to cell signaling and manipulation of key enzymes that affect protein acylation.

Previous Research Activities or Publications with Medical Students:

Camp, L.A., and Hofmann, S.L. Purification and Properties of a Palmitoyl-Protein Thioesterase that Cleaves Palmitate from H-Ras. J. Biol. Chem. 268: 22566-22574 (1993).

Camp, L.A., Verkruyse, L.A., Afendis, S.J., Slaughter, C.S. and Hofmann, S.L. Molecular Cloning and Expression of Palmitoyl-Protein Thioesterase. J. Biol. Chem. 269: 23212-23219 (1994).

Verkruyse, L.A. and Hofmann, S.L. Lysosomal Targeting of Palmitoyl-Protein Thioesterase. J. Biol. Chem. 271: 15831-15836 (1996).

Lu, J.-Y., Verkruyse, L.A., and Hofmann, S.L. Lipid Thioesters Derived from Acylated Proteins Accumulate in Infantile Neuronal Ceroid Lipofuscinosis: Correction of the Defect in Lymphoblasts by Recombinant Palmitoyl-Protein Thioesterase. Proc. Natl. Acad. Sci. U.S.A. 93: 10046-10050 (1996).

Verkruyse, L.A., Natowicz, M.R, and Hofmann, S.L. Palmitoyl-Protein Thioesterase Deficiency in Fibroblasts of Individuals with Infantile Neuronal Ceroid Lipofuscinosis and I-Cell Disease. Biochim. Biophys. Acta 1361:1-5 (1997).

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