Electron Microscopy reconstruction of the yeast vacuolar ATPase. Ribbon models for individual protein subunits have been fit to the electron density.
From the lab of Stephan Wilkens, PhD.
David W Pruyne, PhD
- Associate Professor of Cell and Developmental Biology
Research Programs and Affiliations
- Biomedical Sciences Program
- Cell and Developmental Biology
Education & Fellowships
- PhD: Cornell University, 1999, Biochemistry, Molecular and Cell Biology
- BS: Cornell University, 1993, Biochemistry
Biochemistry and cell biology of formins as actin cytoskeleton organizers, using Caenorhabditis elegans as a model system.
- American Society for Cell Biology (ASCB)
Link to PubMed (Opens new window. Close the PubMed window to return to this page.)
The actin cytoskeleton is a network of filaments composed of the protein actin that populate the cell's cytoplasm. In a given cell, this network can be organized into a large number of distinct substructures that may range form from simple cable-like bundles through complex, repetitive arrays. These cytoskeletal structures give cells their proper shape, control the distribution of organelles, and allow cells to move. Our primary goal is to understand at the molecular level how distinct actin filament structures assemble, and how they perform their functions. Our focus is on the family of actin-organizing proteins called Formins. Formins are conserved proteins with homologs in nearly every type of eukaryotic organism, including animals, plants, and fungi. Among animals, seven distinct subclasses of Formins exist, but their precise functions are not clear. We are probing the functions of these Formin subclasses through a combination of biochemical assays using purified proteins, and genetic and microscopic studies using the model organism Caenorhabditis elegans. Our current work focuses on the relationship between one Formin subclass and muscle development.
SUNY Distinguished Professor Emeritus
- Richard Cross, PhD
- David Turner, PhD