Protein Prenylation: the Anchor of Life

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What is Protein Prenylation?

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

Work 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 and cell culture and animal-based work.  The goal of this work 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.

Group News

Shelby Auger receives Traineeship from Functional Proteomics of Aging NIH Training Grant

Shelby Auger received a two year traineeship from the Functional Proteomics of Aging NIH Training Grant.  That grant (An NIH T32 Training Grant) provides a two year stipend and additional training in proteomics, aging research and bioinformatic analysis.  Congratulations, Shelby!

Yiao Wang Defends Ph.D. Thesis

Yiao Wang (now Dr. Yaio Wang!) successfully defended his thesis entitled "Prenylated Chemically Self-Assembled Nanorings: A Versatile Platform for Macro-Chemical Biology". Yiao carried out pioneering work in the area of chemically self assembled nanorings and was a joint student coadvised by Dr. Wagner in Medicinal Chemistry.  Yiao took a position at Biothera in the Twin Cities, a clinical stage immuno-oncology company developing focused on immunotherapy.

2021 Summer visitors

The Distefano group was fortunate to host three visitors this summer.  Holly Passetti, a chemistry and biology major from Alfred University participated in our UMN Lando/NSF program.  She worked on using peptide libraries to probe prenyltransferase specificity.  Holly is off to graduate school this fall.  Claire Hypolite and Eva Nelson, both high school teachers at Edison High School, worked on developing a high school science experiment based on the metabolic labeling work being done in the group.  They will be returning next summer!

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