Research Information

My background is in simulating collective behavior in animal groups, and I came to Peifer lab to learn the experimental  approaches to define molecular mechanisms and also to continue learning about the dynamics of living systems.  I am exploring how Cadherin-based adherens junctions (AJs) promote coordinated behavior in epithelial cells by facilitating a connection between the apical membranes and actomyosin cytoskeletons of neighboring cells. The proper assembly, positioning, and function of AJs requires assembly of a large multiprotein machine at the apicolateral membrane, via interactions between specific domains of these proteins.

Canoe (Cno) is a large scaffolding protein and is an orthologue of the mammalian protein Afadin. Cno protein  contains multiple structural domains and a long intrinsically disordered region (IDR).  I am collaborating with Dr. Corbin Jensen, Prof. Mark Peifer, Leah Wolfsberg and Prof. Kevin Slep to characterize mutants where regions of the IDR are altered,  using quantitative confocal microscopy.

When we delete Canoe’s intrinsically disordered region (IDR), the mutants show drastically altered protein localization, with reduced localization to the cytoskeleton-adhesion interface, and instead, strong localization to nuclei.  They also exhibit defects in tissue integrity during development, but these are not as severe as those of mutants totally lacking Canoe. Given that the IDR appears indispensable, we are now investigating hypotheses of the molecular-to-tissue level relationship through literature on the functions of IDRs: binding motif, linker/spacer, multivalent assembly, entropic sensing and crowding.