Honors College

Document Type

Honors Thesis

Publication Date



Palmitoylation is a reversible, post translational, lipid modification performed by proteinacyltransferases (PAT). PATs are membrane-bound enzymes which contain a conserved region that is rich in cysteine residues and contains a DHHC (Asp-His-His-Cys) conserved domain. This region is involved in the transfer of a 16-carbon palmitate from palmitoyl-CoA to a target protein. Palmitoylation plays many important functions such as targeting the protein to a lipid raft, shuttling the target protein or anchoring it to the cell membranes as well as aiding in the three dimensional folding of the protein. This process plays an important role in signal transduction, anchoring and cellular timing. Palmitoylation has been shown to play a role in schizophrenia, hormone dysfunction, intellectual disability, Huntington’s disease and cancer. In order to study PATs, genetic knock-ins were created using YFP (a yellow fluorescent protein) in order to study expression patterns in growing Dictyostelium discoideum, a soil amoeba whose multi-stage life cycle is highly dependent on the action of palmitoylated heterotrimeric G-proteins. This method for studying the expression pattern of PATs provides accurate information about both the timing of expression and the location of expression in living dictyostelium. This research will help to provide a basic understanding of how Dictyostelium makes use of its PAT’s through providing a ‘when’ and ‘where’ for their expression. This data will allow for a more educated inspection of the ‘why’ and ‘how’ questions associated with PATs and their substrates.