Protein Prenylation - The Anchor of Life
Protein prenylation is a post-translational modification that consists of the attachment of 15 or 20 carbon isoprenoids to specific cysteine residues positioned near the C-termini of proteins. In a eukaryotic cell, there are several hundred prenylated proteins including most members of the Ras superfamily and heterotrimeric G-proteins; the prenyl group serves to anchor these proteins in the membrane so that they are positioned to interact with cell surface receptors either directly or via adaptor proteins. This means that essentially all signaling processes in eukaryotic cells require the participation of prenylated proteins for everything ranging from the regulation of cell division to stem cell differentiation and development. Beyond biological significance, the critical role of prenylated proteins also makes them important targets for the design of new therapeutic agents for a variety of diseases.
Research in the Distefano Group
Works in the Distefano Group on protein prenylation is focused in two areas: Chemical Biology and Biotechnology Applications. In pursuit of those studies, members of the group perform a variety of different types of experiments including chemical synthesis, biochemistry, proteomics, cell culture and animal-based work. The goal of these works is to gain insight into protein prenylation that can be used to advance biology and develop new therapeutic approaches for a broad range of diseases including cancer, Alzheimer’s disease and infectious disease.
Research Highlights
MDD Group News
Kevin Park defends Ph.D. thesis
Kevin recently defended his Ph.D. thesis entitled “ENZYMATIC PROTEIN LABELING AND POLYMERIC MATERIALS FOR CANCER-THERAPY AND ANTI-FOULING APPLICATIONS”
Congratulations! Kiall Suazo defends thesis
Congratulations to Kiall Suazo (Now Dr. Kiall) for successfully defending his Ph.D. thesis today entitled "Applications of chemical proteomics in defining prenylated prenylomes and discovering novel prenylated proteins". Kiall has been a dynamo of activity spearheading our efforts in mass spectrometry-based proteomic analysis of prenylated proteins. He will remain in Minnesota for the next month finishing things up before starting a postdoctoral position at Pacific Northwest National Laboratory in the group of Aaron Wright. Congratulations Kiall! We will miss you.
Thiol uncaging at wavelengths greater than 800 nm
In work recently featured on the cover of Organic and Biomolecular Chemistry, spearheaded by postdoc Matt Hammers along with other undergraduates, graduate students and postdocs from the research groups of Mark Distefano, David Blank (UMN) and Zach Ball (Rice U.), the development of protecting groups for sulfur that can be removed at wavelengths greater than 800 nm is described. Such protecting groups have great potential for applications in biology and material science.