Avery Mathias
Background & Contact Information
Position (2024 – Present)
Education: B.A. Bates College Biology and Art
Fellowships & Awards: Kerry Grant Award for a thesis in Biology
Email: ajmath@unc.edu
Research Information
My background is in the use of sponges as natural biomonitors to measure freshwater biodiversity. In the Horton lab, we collected freshwater sponge samples and used metabarcoding to identify freshwater sponge species from diverse aquatic habitats. We piloted experiments testing animal-specific eDNA primers to create libraries for eDNA sequencing. Then we used a bioinformatics pipeline to analyze eDNA sequences from one freshwater sponge species to determine its effectiveness as a biomonitoring target of fish and other animal species.
I joined the Peifer lab to delve further into cell biology using Drosophila as a model organism. Cadherin-based adherens junctions (AJs) support coordinated activity in epithelial cells by linking the apical junctions to the actomyosin cytoskeletons of adjacent cells. A complex multiprotein structure must form at the apicolateral membrane, involving multivalent interactions via different protein domains in order for the AJs to assemble, position, and function properly. These interactions are both dynamic and robust during embryonic development as the embryo and its cells are constantly changing shape while the cytoskeleton exerts significant force on cell-cell contacts. Disruption of these connections can impact multiple morphogenetic processes, including gastrulation, germband extension, and dorsal closure. Research revealed that the relationship between AJs and the cytoskeleton involves a complex network of proteins rather than a linear pathway.
Canoe (Cno) is a large scaffolding protein in Drosophila that is the homolog of the mammalian protein Afadin. Cno and Afadin share multiple folded protein domains and intrinsically disordered region (IDR) which comprises over a third of the total protein. Earlier work in the lab explored the function of most of the folded domains, revealing a key role for one of the Rap1-binding RA domains but also revealing surprising robustness, with mutants individually lacking three of the five folded domains viable and fertile.
We thus are exploring the role of the IDR in Cno function. We have generated mutants that remove the IDR from Cno in vivo and have found that this significantly reduces Cno’s function and disrupts its localization to cell junctions. This results in disrupted tissue integrity during development. I am currently examining mutants that dissect different regions of the IDR to further investigate its role in embryonic development and the interaction between junctions and the cytoskeleton, combining powerful genetic tools and using confocal microscopy.
Publications