Tools for the modulation and identification of protein prenylation
Abstract
Protein prenylation is an essential posttranslational modification for many important signaling molecules. Prenyl addition anchors the protein to membranes by a large hydrophobic lipid handle. Without this addition many essential cellular proteins would become mislocalized and lose the ability to properly function. Synthetic small molecules have been developed to target the protein farnesyltransferase to combat certain type of cancer by knocking-out Ras function. These FTIs have led to interesting clinical results not anticipated. The development of tools that could selectively modulate the prenylation event would be useful tools to determine the mechanism of FTI function and to determine the roles of individual farnesylated proteins. Also tools that could be used to selectively identify cellular proteins that are modified via farnesylation would be of great value a prenylomic approach was developed as such a tool.
Degree
Ph.D.
Advisors
Gibbs, Purdue University.
Subject Area
Biochemistry|Pharmacology
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