Biological Sciences

Biological Science Faculty Research

Deborah Chadee


Assistant Professor
Office: WO3235
Phone: 419-530-4159


The research in our lab focusses on how epithelial cells found throughout the human body remodel their actin cytoskeleton during differentiation to attain their specific cellular shapes. As a model system, we look at how the epithelial cells of the human gut remodel their surface to form a structure known as the "brush border". The brush border is a tightly packed collection of apical microvilli; small membrane protrusions that are supported by the actin cytoskeleton. These apical microvilli are in direct contact with the luminal contents of the intestine and are responsible for all the nutrient absorption that occurs in our digestive tract.

Specifically, we are interested in:
(1) Understanding the fundamental mechanisms that underlie brush border assembly, with particular regard to identifying the proteins and signaling pathways that control it.
(2) How defects in these proteins and pathways cause human disease.

Students in the lab receive hands-on training in diverse areas including molecular biology, protein biochemistry and enzymology, structural biology and high-resolution fluorescence and electron microscopy.

Current Students

Maura Graves, Ph.D. candidate

Samaneh Matoo, Ph.D. candidate

Acharya Prashun, Ph.D. candidate



Selected publications:

Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin, D.A., Tyska M.J. (2016) ANKS4B is essential for intermicrovillar adhesion complex formation. Dev Cell. 36(2), 190-200.

Crawley S.W., Mooseker, M.S., Tyska M.J. (2014) Shaping the Intestinal Brush Border. The Journal of Cell Biology. 207(4), 441-451.

Crawley S.W., Shifrin, D.A., Grega-Larson N.E, McConnell, R.E., Benesh, A.E., Mao S., Zheng Y., Zheng, Q.Y., Nam K.T., Millis B.A., Kachar B., Tyska M.J. (2014) Intestinal brush border assembly driven by protocadherin-based intermicrovillar adhesion links. Cell. 157(2), 433-46.

Crawley S.W.*, Liburd J.*, Shaw K., Jung Y., Smith S.P., Côté G.P. (2011) Identification of calmodulin and MlcC as light chains for Dictyostelium myosin-I isozymes. Biochemistry. 50(30), 6579-88.
*Contributed equally to this work.

Crawley S.W., Samimi Gharaei M., Ye Q., Yang Y., Raveh B., London N., Schueler-Furman O., Jia Z., Côté G.P. (2010) Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the -kinase domain. J Biol Chem. 286, 2607–2616.

Ye, Q*., Crawley S.W.*, Yang, Y., Côté G.P., Jia Z. (2010) Crystal Structure of the -kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A. Science Signaling. 3, ra17.
*Contributed equally to this work.

Crawley S.W., Côté G.P. (2009) Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain. Biochem J. 420, 115-22.

Crawley S.W., Côté G.P. (2008) Determinants for substrate phosphorylation by Dictyostelium myosin II heavy chain kinases A and B and eukaryotic elongation factor-2 kinase. Biochim Biophys Acta. 1784, 908-15.

Crawley S.W., de la Roche M.A., Lee S.F., Li Z., Chitayat S., Smith S.P., Côté G.P. (2006). Identification and characterization of an 8-kDa light chain associated with Dictyostelium discoideum MyoB, a class I myosin. J Biol Chem. 281, 6307-15.

Last Updated: 2/15/21