Our research group is interested in the molecular mechanisms underlying the assembly, regulation, and function of the septin family of proteins in budding yeast. The septins are a widely conserved GTP-binding protein family that can polymerize into a variety of cellular geometries. They function in vivo by promoting and sensing membrane curvature, serve as a barrier between membrane-enclosed compartments, and recruit many scores of additional proteins that localize to the division site during the cell cycle. We are interested in addressing a number of questions regarding the molecular mechanisms that govern both assembly and regulation of this protein complex, and characterize the direct binding partner(s) that associate with the septin structure within the cell (such as the kinases responsible for control of cell cycle progression). We employ a combination of experimental approaches including genetics, molecular and cell biology, biochemistry, and molecular evolutionary techniques. Additionally, our lab is interested in utilizing CRISPR/Cas technology to further advance the application and regulation of this powerful gene editing platform using yeast as a model system.
[Top Left, Schematic of the septin organization during yeast cell cycle. Figure adapted from Kinoshita, 2006, Current Opinion in Cell Biology, 18, 54-60. Copyright © 2016 Elsevier Ltd. Reproduced with permission from Elsevier. Top Right, Model of the budding yeast septin hetero-octamer complex during mitosis; Bottom Left, Serial dilution growth assay of yeast strains, Bottom Right, Fluorescence microscopy of live yeast cells (1000x mag.) visualizing two subunits of the septin complex. Data images from Finnigan et al., 2015, Genetics 200, 821-841. Reproduced with permission from the Genetics Society of America.]