Faculty

William E. Balch 
Professor
Department of Cell Biology
TSRI - 1988

Joint Appointments 
MOLECULAR BIOLOGY

Education 
Ph.D., University of Illinois, 1979

Research Focus 
Molecular basis for membrane trafficking
and protein folding disease

Our laboratory is interested in understanding the rules that direct protein traffic through secretory pathway of eukaryotic cells. We use structural, biochemical, morphological and molecular tools to study mechanisms of protein folding and protein-protein interactions that mediate membrane vesicle targeting and fusion. We are particularly interested in defining the key trafficking defects that lead to hereditary amyloid disease, childhood emphysema, and cystic fibrosis, all diseases related to the inability of specific proteins to be properly transported to their site of function in the cell.

Selected References 
Wang, X., J. Matteson, Y. An, B.D. Moyer, J.S. Yoo, S. Bannykh, I.A. Wilson, J.R. Riordan, and W.E. Balch. COPII-dependent export of cystic fibrosis transmembrane conductance regulator (CFTR) from the ER utilizes a di-acidic exit code. J. Cell Biol. 2004. In press.

Alory, C., and W.E. Balch. Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily. Mol. Biol. Cell 14:3857-3867, 2003.

Kelly, J.W., and W.E. Balch. Amyloid as a natural product. J. Cell Biol. 161:461-462, 2003.

Huff, M.E., L. Page, W.E. Balch, and J.W. Kelly. Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of Finnish type. J. Mol. Biol. 334:119-27, 2003.