Our lab has a long-standing interest in the mechanisms by which the actin cytoskeleton exerts forces to move membranes in cells. We are elucidating general principles of actin function using clathrin-mediated endocytosis as a representative process. We use the budding yeast Saccharomyces cerevisiae as a model organism because these cells have an unusually stringent requirement for actin assembly during clathrin-mediated endocytosis and are accessible with biochemical-, genetic-, and microscopy-based experiments. During clathrin-mediated endocytosis in budding yeast, a burst of actin assembly and myosin activity generates the driving force for membrane invagination.
Current research interests in the lab involve determining how actin assembly is initiated and coordinated with myosin activity at endocytic sites and developing semi in vitro assays for studying clathrin-mediated endocytosis in crude lysates.
Sun, Y., Leong, N. T., Jiang, T., Tangara, A., Darzacq, X., & Drubin, D. G. (2017). Switch-like Arp2/3 activation upon WASP and WIP recruitment to an apparent threshold level by multivalent linker proteins in vivo. eLife, 6.
Miao, Y., Han, X., Zheng, L., Xie, Y., Mu, Y., Yates III, J. R., & Drubin, D. G. (2016). Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast. Nature communications, 7.
Lewellyn, E. B., Pedersen, R. T., Hong, J., Lu, R., Morrison, H. M., & Drubin, D. G. (2015). An engineered minimal WASP-myosin fusion protein reveals essential functions for endocytosis. Developmental cell, 35(3), 281-294.
Sun, Y., Leong, N. T., Wong, T., & Drubin, D. G. (2015). A Pan1/End3/Sla1 complex links Arp2/3-mediated actin assembly to sites of clathrin-mediated endocytosis. Molecular biology of the cell, 26(21), 3841-3856.