Poster Title (Current Submission)
Major(s)
Biochemistry
Minor(s)
Spanish
Mentor Name
Kris DeMali
Mentor Department
Biochemistry
Abstract
Extracellular matrix connections of integrins and actin-binding proteins such as vinculin are crucial elements of human health. Interruptions of these linkages contribute to the progression of numerous diseases including cancer, heart disease, and some muscular dystrophies. We have recently identified a short vinculin activating peptide (VAP), comprised of three vinculin binding sites (VBS) that increase integrin-mediated adhesion to fibronectin or collagen. Using a series of truncation mutants, we have mapped the residues sufficient for binding vinculin. We are investigating the mechanism by which the vinculin activating peptide increases adhesion and how these effects regulate integrin activity. These studies provide insight into how vinculin activation regulates integrin function and will open up new therapeutic possibilities.
Examining the Effects of VAP on Vinculin
Extracellular matrix connections of integrins and actin-binding proteins such as vinculin are crucial elements of human health. Interruptions of these linkages contribute to the progression of numerous diseases including cancer, heart disease, and some muscular dystrophies. We have recently identified a short vinculin activating peptide (VAP), comprised of three vinculin binding sites (VBS) that increase integrin-mediated adhesion to fibronectin or collagen. Using a series of truncation mutants, we have mapped the residues sufficient for binding vinculin. We are investigating the mechanism by which the vinculin activating peptide increases adhesion and how these effects regulate integrin activity. These studies provide insight into how vinculin activation regulates integrin function and will open up new therapeutic possibilities.