Center for Membrane and Cell Physiology and Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22903, USA
Stefanie S. Schmieder
Division of Gastroenterology, Boston Children’s Hospital, Boston, MA 02115, USA
Krishnan Raghunathan
Department of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15224, USA
Ajit Tiwari
Center for Membrane and Cell Physiology and Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22903, USA
Ting Wang
Center for Membrane and Cell Physiology and Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22903, USA
Christopher V. Kelly
Department of Physics and Astronomy, Wayne State University, Detroit, MI 48201, USA
Wayne I. Lencer
Division of Gastroenterology, Boston Children’s Hospital, Boston, MA 02115, USA
Cholera toxin B-subunit (CTxB) has emerged as one of the most widely utilized tools in membrane biology and biophysics. CTxB is a homopentameric stable protein that binds tightly to up to five GM1 glycosphingolipids. This provides a robust and tractable model for exploring membrane structure and its dynamics including vesicular trafficking and nanodomain assembly. Here, we review important advances in these fields enabled by use of CTxB and its lipid receptor GM1.
