ASU SoLS Faculty: Jeanne Wilson-Rawls

Molecular Biology

I am interested in studying the role of the Notch signaling pathway in cell lineage decisions. The Notch signaling pathway is highly conserved from flies to mammals and it regulates the differentiation of many cell types. In my lab, we are currently studying the role of Notch signaling in folliculogenesis and gonadal development. We use a variety of approaches from biochemical assays to the study of the phenotypes of a targeted null mouse mutant of the gene lunatic fringe and tissue targeted transgenics of Notch2 mutants.

Selected Publications

Fischer, C., J. Johnson, B. Stillwell, Z. Cerovac, J. Conner, J. Wilson-Rawls and A. Rawls. (2004). ATF4 is required for the differentiation of the lamina propria layer of the vas deferens. Biol. Reprod. 70, 371-378.

Rhee, J.M., Takahashi, Y., Saga, Y., Wilson-Rawls, J., and Rawls, A. (2003). The protocadherin papc is required for epithelialization along the segmental border during mouse somitogenesis. Dev Biol 254, 248-261

Johnson, J., McGaughey, R.W., Rawls, A., Wilson-Rawls, J. (2001) Notch pathway genes are expressed in developing mammalian ovarian follicles. Mech Dev 109, 353-359

Rawls, A., McGaughey, R. W., and J. Wilson-Rawls. (2001). Developmental History of the mammalian oocyte: Insight from mouse mutations. Front Biosci 6, D1173-1185.

Rawls, A., Wilson-Rawls, J., and E.N. Olson. (2000). Genetic control of Somite formation. Curr. Top. Dev. Biol. 47,131-54.

Wilson-Rawls, J., Molkentin, J.D., Black, B.L., and E.N. Olson. (1999). Activated notch inhibits myogenic activity of the MADS-Box transcription factor myocyte enhancer factor 2C. Mol. Cell. Biol. 19:2853-2862.

Wilson-Rawls J., C. R. Hurt, S. M. Parsons and A. Rawls. (1999). Differential regulation of epaxial and hypaxial muscle formation by Paraxis. Development 126, 5217-29

Wilson-Rawls, J., J. Liu, P.N. Laneuville, and R.B. Arlinghaus. 1996. P210 Bcr-Abl interacts with the interleukin-3 beta c subunit and constitutively induces its phosphorylation. Cancer Res. 56:3426-3430.

L.K. Hawkins, Wilson-Rawls, J., and W.S.M. Wold. 1995. Region E3 of subgroup B human adenoviruses encode a 16,000 MW membrane protein that may be a distant analog of the E3 6.7K protein of subgroup C adenoviruses. J. Virol. 69:4292-4298.

Wilson-Rawls, J., S.L. Deutscher, and W.S.M. Wold. 1994. The signal-anchor domain of adenovirus E3-6.7K, a type III integral membrane protein, can direct adenovirus E-3gp19K, a type I integral membrane protein, into the membrane of the endoplasmic reticulum. Virology 201:66-76.

Wilson-Rawls, J. and W.S.M. Wold. 1993. The E3-6.7K protein of adenovirus is an Asn-linked integral membrane glycoprotein localized in the endoplasmic reticulum. Virology 195:6-15.

Wilson-Rawls, J., S.K. Saha, P. Krajcsi, A.E. Tollefson, L.R. Gooding and W.S.M. Wold. 1990. A 6700 MW membrane protein is encoded by region E3 of adenovirus type 2. Virology 178, 204-212.