Education

B.S., Chemistry, University of South Dakota, Vermillion, SD, 2003
Ph.D., Medicinal Chemistry and Molecular Pharmacology, Purdue University, Lafayette, IN, 2008
2nd year FIRST Postdoctoral Fellow, 2008 - present

Research Statement

Understanding muscle structure, function, and assembly using C. elegans as a model system - The basic mechanism of muscle contraction is understood; however, the mechanism of assembly and function is not well understood.  We study the giant protein kinases including twitchin, UNC-89, and TTN-1 in C. elegans. This class of proteins is critical for normal muscle structure and function, but study of these proteins has been hampered because of their large size.  Human homologues of the giant protein kinases and their associated proteins have been demonstrated to be important for human diseases including muscular dystrophy, and blindness.

unc-89 mutants display disorganized myofibrils, especially at the A-band, and usually lack M-lines. unc-89 can be alternatively spliced to result in 6 different polypeptides ranging in size from 156,000 to 900,000 Da. The largest of these isoforms consists of 52 Ig domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains near their N-termini, and two protein kinase domains (called PK1 and PK2) near their C-termini. The human homolog of UNC-89 is called obscurin. Although there are many mutant alleles of unc-89 available, given the size of the protein and its gene (>60 kb), it is difficult to use these mutants to characterize the function of each domain. Thus, we have taken the approach of identifying and learning the functions of the binding partners of UNC-89 domains as a way to gain insight into the function of UNC-89.

Publications

Wilson, K.J., Gilmore, J.L., Foley, J., Lemmon, M.A., Riese, D.J. (2009) Functional selectivity of EGF family peptide growth factors: Implications for cancer. Pharmacol Ther.  doi:10.1016/j.pharmthera.2008.11.008.

Willmarth, N.E., Baillo, A., Dziubinski, M.L., Wilson, K., Riese, D.J. 2nd, Ethier, S.P. (2009) Altered EGFR localization and degradation in human breast cancer cells with an amphiregulin/EGFR autocrine loop. Cell Signal. 21(2):212-9.

Wilson, K.J., Mill, C.P., Cameron, E.M., Hobbs, S.S., Hammer, R.P., Riese, D.J. 2nd. (2007) Inter-conversion of neuregulin2 full and partial agonists for ErbB4. Biochem Biophys Res Commun. 14;364(2):351-7.

Ristic, Z., Wilson, K., Nelsen, C., Momcilovic I., Kobayashi, S., Meeley, R., Muszynski, M., Habben, J. (2004) A maize mutatn with decreased capacity to accumulate chloroplast protein synthesis elongation factor (EF-Tu) displays reduced tolerance to heat stress. Plant Sci. 167: 1367-1374. 

Emory University School of Medicine
Pathology Department
Whitehead Biomedical Research Bldg.
615 Michael STreet
Atlanta, GA 30322
Tel: (404) 727-5945
Email: kjwils2@emory.edu