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Cancer and metastasis are associated with abnormal cellular signaling. Our goal is to understand how the Rho family of signaling proteins function in normal cells and how their signaling is altered in cancer and metastasis. In addition, we are applying novel high-throughput screening methods to identify drug-like molecules that target Rho signaling pathways. We use these compounds to study protein function in the laboratory and to validate new therapeutic approaches to cancer.

1. Strochlic TI, Concilio S, Viaud J, Eberwine R, Wong LE, Minden A, Turk BE, Plomann M, Peterson JR. Identification of neuronal substrates implicates Pak5 in synaptic vesicle trafficking. Proc Natl Acad Sci USA (In press).
2. Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR. Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat Biotechnol. 2011;29:1039-45. PubMed
3. Delorme-Walker VD, Peterson JR, Chernoff J, Waterman CM, Danuser G, DerMardirossian C, Bokoch GM Pak1 regulates focal adhesion strength, myosin IIA distribution and actin dynamics to optimize cell migration. J Cell Biol. 2011;193:1289-303. PubMed
4. Strochlic TI, Viaud J, Rennefahrt UEE et al. Phosphoinositides are essential co-activators for p21-activated kinase 1 (Pak1). Mol Cell. 2010;40(3):493-500. PubMed
5. Viaud J and Peterson J. An allosteric kinase inhibitor binds the p21-activated kinase (Pak) autoregulatory domain covalently. Mol Cancer Ther. 2009;8(9):2559-65. PubMed
6. Deacon SW, Beeser A, Fukui JA et al. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem Biol. 2008;15(4):322-31. PubMed