Protein Dynamics Involved in the Cytokinesis of Fission Yeast

Cytokinesis is the final stage of cell division when eukaryotes assemble a contractile acto-myosin ring to physically divide their cytoplasm and genetic material to create two daughter cells. Global and local concentrations of protein components involved in the contractile ring assembly of fission yeast have been using quantitative fluorescence microscopy [1]. However, the dynamics of the ring protein remains unknown due to the limitations of conventional imaging and image analysis approaches. In this project, we use highly integrated computational-experimental research approaches that consist of high-resolution imaging with the assistance of micro-well arrays manufactured in MTL, computational image analysis (using an image-correlation spectroscopy algorithm) [2] [3], and data-driven computational modeling. Our goal is to establish a molecular-level model that describes mechanistically how the core set of ring proteins in fission yeast is organized prior to, as well as during, its constriction in cytokinesis. Specifically, the summer project includes an experimental imaging part and a computational modeling part.


References
  1. Wu, K.Y., et al., Local translation of RhoA regulates growth cone collapse. Nature, 2005. 436(7053): pp. 1020-1024. []
  2. Kolin, D.L. and P.W. Wiseman, Advances in image correlation spectroscopy: Measuring number densities, aggregation states, and dynamics of fluorescently labeled macromolecules in cells. Cell Biochemistry and Biophysics, 2007. 49(3): p. 141. []
  3. Sisan, D.R., et al., Spatially resolved fluorescence correlation spectroscopy using a spinning disk confocal microscope. Biophysical Journal, 2006. 91(11): p. 4241. []

Microsystems Technology Laboratories | Massachusetts Institute of Technology | 60 Vassar Street, 39-321 | Cambridge, MA 02139 | http://www.mtl.mit.edu
Copyright © Massachusetts Institute of Technology. | Information on MIT Accessibility