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.

This document is currently not available here.

Share

COinS
 
Apr 13th, 10:00 AM Apr 13th, 11:00 AM

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.