Research Interest
Formins are a highly conserved family of proteins that nucleate actin filaments in an Arp2/3-independent manner. In budding yeast, the formin Bni1 assembles actin cables that anchor to the cortex of the bud site and radiate into the mother cell. My research will address the question of how Bni1 is assembled into cables by examining the behavior in vivo of Bni1-GFP. By examining the movements of full-length and truncation constructs, comparisons of the rate of Bni1 movement and the rate of cable assembly can be made. Secondly, I plan to examine the regulation of Bni1-dependent actin assembly in vivo. I will use traditional biochemical approaches to identify binding partners and post-translational modifications of Bni1.
Education
| 2004–present | Postdoctoral fellowship in the laboratory of David Pellman, Dana Farber Cancer Institute |
| 2003 | PhD, Florida State University. Tallahassee, Florida |
| 1996 | BA, New College. Sarasota, Florida |
Selected publications
- Buttery, S., Yoshida, S., and Pellman, D. Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables. Mol Biol Cell (2007) May;18(5):1826-38li>
- Yi, K., Buttery, S., Stewart, M., Roberts, T., p34, a Ser/Thr kinase in the MSP motility apparatus, is required for leading edge protrusion in the amoeboid sperm of Ascaris. Submitted to MBC.
- Grant, R.P., Buttery, S.M., Ekman, G.C., Roberts, T.M., and M. Stewart. Structure of MFP2 and its Function in Enhancing MSP Polymerization in Ascaris Sperm Amoeboid Motility. Journal of Molecular Biology. 347: 583-595.
- Buttery SM, Ekman GC, Seavy M, Stewart M, & Roberts TM. Dissection of the Ascaris Sperm Motility Machinery Identifies Key Proteins Involved in MSP-Based Amoeboid Locomotion. Mol Biol Cell (2003), 14, 5082–88
