Event Title
Regulation of the Diaphanous-Related Formin, DAAM1 in Mammalian Cells
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry
Mentor Information
Brad Wallar, wallarb@gvsu.edu
Department
Chemistry
Location
Kirkhof Center KC16
Start Date
13-4-2011 10:00 AM
End Date
13-4-2011 11:00 AM
Keywords
Life Science, Physical Science
Abstract
Diaphanous-related formins (DRFs) are involved in the regulation of the cytoskeleton and are highly conserved across many species. DRFs are regulated through a mechanism of autoinhibition, in which the two ends of the protein bind to each other to lock it in an inactive conformation. Under highly regulated cellular conditions, DRF autoinhibition is disrupted by the binding of other cellular proteins, which causes the activation of the DRF proteins. Here, we have studied the regulation of a specific DRF protein, DAAM1, which has been shown to be critical for cellular processes in neurons. Using a combination of site-directed mutagenesis, protein biochemistry, fluorescence anisotropy, and immunofluorescence imaging, we have construced a constitutively active DAAM1 protein that sheds light on the location and function of DAAM1 in cells. In addition, we have identified specific amino acid residues on DAAM1 that are essential for its regulation.
Regulation of the Diaphanous-Related Formin, DAAM1 in Mammalian Cells
Kirkhof Center KC16
Diaphanous-related formins (DRFs) are involved in the regulation of the cytoskeleton and are highly conserved across many species. DRFs are regulated through a mechanism of autoinhibition, in which the two ends of the protein bind to each other to lock it in an inactive conformation. Under highly regulated cellular conditions, DRF autoinhibition is disrupted by the binding of other cellular proteins, which causes the activation of the DRF proteins. Here, we have studied the regulation of a specific DRF protein, DAAM1, which has been shown to be critical for cellular processes in neurons. Using a combination of site-directed mutagenesis, protein biochemistry, fluorescence anisotropy, and immunofluorescence imaging, we have construced a constitutively active DAAM1 protein that sheds light on the location and function of DAAM1 in cells. In addition, we have identified specific amino acid residues on DAAM1 that are essential for its regulation.