Dr. Gregory Hudalla, Dr. Edward Phelps, and lab members’ recent work, “Physical tuning of galectin-3 signaling,” has been published by the National Academy of Sciences Proceedings of Sciences the United States of America (PNAS).
- Shaheen A. Farhadi, Ph.D., postdoctoral researcher, Hudalla Lab
- Renjie Liu, Ph.D., postdoctoral researcher, Hudalla Lab
- Mithra Becker, Ph.D. student, Phelps Lab
- Edward Phelps, Ph.D., Assistant Professor & J. Crayton Pruitt Family Term Fellow, Department of Biomedical Engineering, University of Florida
- Gregory Hudalla, Ph.D., Associate Professor, Department of Biomedical Engineering, University of Florida
The family of carbohydrate-binding proteins known as galectins receive considerable attention for their ability to modulate cell behavior in both normal and pathological settings. Galectin-3, for instance, can crosslink membrane glycans to initiate, amplify, attenuate, or inhibit signal transduction pathways that lead to cell differentiation, proliferation, or death. However, understanding structure–function relationships of galectin-3 is challenged by its promiscuous glycan-binding properties and assembly into oligomers with undefined number of subunits or “valency.” Here, we address these challenges by providing a toolbox of synthetic galectin-3 oligomers with tunable valency. Cell-based studies with these oligomers suggest a role for physical size as a structural determinant of galectin-3 signaling function, in addition to the increased binding strength typically associated with multivalency.