Andrew Berglund, Ph.D.



Research:  Regulation of RNA processing and molecular mechanisms of neurological disease

Ph.D. from Brandeis University, 1997

Contact Information:

     Office: CGRC 255
     Lab:  CGRC 280G
     Telephone:  (352) 273-7888


Professor Berglund earned his Ph.D. degree in Biochemistry from Brandeis University for his work on protein-RNA interactions in pre-mRNA splicing with Michael Rosbash. He joined the laboratories of Steve Schulz and Tom Cech at the University of Colorado where he used x-ray crystallography to study protein-RNA and RNA-RNA interactions. In 2002, Dr. Berglund joined the faculty in the Department of Chemistry & Biochemistry and Institute of Molecular Biology at the University of Oregon. From 2013 to 2015, Dr. Berglund served as Associate Dean and Interim Dean (2014-2015) of the Graduate School at the University of Oregon. He joined the faculty in the Department of Biochemistry & Molecular Biology at the University of Florida in 2015.


The Berglund lab uses a broad range of approaches to study the molecular mechanisms of neurological diseases that are caused by microsatellite repeat expansions. For many of these diseases (myotonic dystrophy, ALS and ataxias), RNA processing (pre-mRNA splicing) pathways are negatively impacted with specific changes in pre-mRNA splicing proposed to lead to symptoms observed in affected individuals. We use biochemical, cellular and genomic assays to understand the mechanisms through which these diseases alter pre-mRNA splicing. The goal of our research is to use the results from these basic studies to identify innovative strategies to reduce or correct the improper pre-mRNA splicing that occurs in the disease state. For example, we have recently shown that small molecules can be used to rescue the mis-splicing in cell and mouse models of myotonic dystrophy. As shown in the image below (courtesy of Leslie Coonrod), the lab primarily focuses on the microsatellite expansions at the cell level (CUG repeat foci found in myotonic dystrophy type I are the yellow spots – aka as foci) to atomic level (crystal structure of CUG repeats). The central panel represents a model of proteins and RNA aggregating that are thought to form the foci. Our recent data suggests that the RNA does not adopt the A-form helical structures shown in the central and right panels when bound by proteins. An important question the lab is addressing is what structure(s) do the RNAs adopt in cells.