Skip to Content
Associate Professor of Biochemistry
Primary Office: 4-632 BSBIowa City, IA 52242
Email: firstname.lastname@example.orgWeb: Fuentes LaboratoryWeb: Google Scholar Citations
BChE, Chemical Engineering, University of DaytonMS, Biology, University of DaytonPhD, Biochemistry, University of Illinois
Post Doctorate, Structural Biology, University of PennsylvaniaPost Doctorate, Structural and Cancer Biology, University of North Carolina
Department of Biochemistry PhDInterdisciplinary Graduate Program in Molecular and Cellular BiologyInterdisciplinary Graduate Program in Translational BiomedicineMedical Scientist Training Program
Research in my laboratory focuses on important problems in signal transduction pertinent to human health. Our approach is interdisciplinary, combining, biochemical, biophysical, cell biological and molecular biology methods to gain insight into the mechanisms governing signal transduction in eukaryotic and prokaryotic systems. The major goal is to elucidate the molecular mechanisms that regulate signal transduction. Our recent work has focused on two systems.
The first system involves the Rho family of GTPases, a subfamily of the well known Ras superfamily. In their active state, Rho GTPases interact with effector proteins to coordinate changes in gene expression and the actin cytoskeleton. Several molecules, including guanine exchange factors (GEFs), regulate the active state of Rho GTPases. Importantly, the aberrant function of GEFs has been associated with developmental anomalies, mental retardation, and human disease. The long-term goal of this research is to understand the detailed molecular mechanism(s) by which GEF proteins regulate the activation of Rho-family GTPases and how their deregulation leads to disease.
The second system centers on bacterial chemosensory in the soil bacterium Myxococcus xanthus. Chemosensory in Myxococcus xanthus is essential for developmental gene expression, biofilm formation, intercellular communication and gliding motility. In collaboration with Dr. John Kirby (U of I, Microbiology) we are elucidating the biochemical and structural basis for Myxococcus xanthus chemosensory signaling.
Center for Biocatalysis and BioprocessingHolden Comprehensive Cancer Center
Chemosensory regulation of a HEAT-repeat protein couples aggregation and sporulation in Myxococcus xanthus.
Specificity residues determine binding affinity for two-component signal transduction systems.
2013 November. 4(6):e00420-13.
High-resolution structure of the Tiam1 PHn-CC-Ex domain.
Acta crystallographica. Section F, Structural biology and crystallization communications.
2013 July. 69(Pt 7):744-52.
A novel pathway spatiotemporally activates Rac1 and redox signaling in response to fluid shear stress.
The Journal of cell biology.
2013 June. 201(6):863-73.
The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics.
Structure (London, England : 1993).
2013 March. 21(3):342-54.
Distinct ligand specificity of the Tiam1 and Tiam2 PDZ domains.
2011 March. 50(8):1296-308.
Structural and thermodynamic analysis of PDZ-ligand interactions.
Methods in enzymology.
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion.
Journal of molecular biology.
2010 May. 398(5):730-46.
Hidden dynamic allostery in a PDZ domain.
Proceedings of the National Academy of Sciences of the United States of America.
2009 October. 106(43):18249-54.
Conservation of side-chain dynamics within a protein family.
Journal of the American Chemical Society.
2009 May. 131(18):6322-3.
Date Last Modified: 06/06/2016 -
Copyright © 2015 The University of Iowa. All Rights Reserved.