2006 25:7646вЂ“9.Дamdinsuren A, Matsushita H, Ito M, Tanaka M, Jin G, Tsukamoto H, et al. RUNX3 protein is overexpressed in human basal cell carcinomas. Salto-Tellez M, Peh BK, Ito K, Tan SH, Chong PY, Han HC, et al. RUNX3 has an oncogenic role in head and neck cancer. Tsunematsu T, Kudo Y, Iizuka S, Ogawa I, Fujita T, Kurihara H et al. RUNX3 functions as an oncogene in ovarian cancer. Lee CWL, Chuang LSH, Kimura S, Lai SK, Ong CW, Yan B, et al. RUNX3 is oncogenic in natural killer/T-cell lymphoma and is transcriptionally regulated by MYC. Selvarajan V, Osato M, Nah GSS, Yan J, Chung TH, Voon DCC, et al. RUNX3 is multifunctional in carcinogenesis of multiple solid tumors.

The emerging role of RUNX3 in cancer metastasis (Review). RUNX3 facilitates growth of Ewing sarcoma cells. 2002 21.Д«ledsoe KL, McGee-Lawrence ME, Camilleri ET, Wang X, Riester SM, van Wijnen AJ, et al. The Runx3 transcription factor regulates development and survival of TrkC dorsal root ganglia neurons. Levanon D, Bettoun D, Harris-cerruti C, Woolf E, Negreanu V, Eilam R et al. Runx3 and Runx1 are required for CD8 T cell development during thymopoiesis. Woolf E, Xiao C, Fainaru O, Lotem J, Rosen D, Negreanu V, et al. Oncogenic role of RUNX3 in head and neck cancer. RUNX transcription factors: orchestrators of development.

Mevel R, Draper JE, Lie-A-Ling M, Kouskoff V, Lacaud G. These results proved that this peptide has the potential to be developed as an efficient therapeutic molecule for targeting RUNX3 Threonine 209 phosphorylation-dependent tumor phenotypes. We also tested the efficacy of this peptide to block the RUNX3 Threonine 209 phosphorylation mediated tumorigenic functions in in vitro cell culture models, patient-derived explant (PDE) models and in in vivo tumor xenograft models. We found that this peptide is stable both in in vitro and in vivo conditions, not toxic to normal cells and inhibits the Threonine 209 phosphorylation in RUNX3 by PAK1. The selection of this specific peptide from multiple possible peptides was based on their binding energies, hydrogen bonding, docking efficiency with the active site of PAK1 and their ability to displace PAK1вЂ“RUNX3 interaction in our prediction models. Based on these proofs and to explore the translational significance of these findings, we designed a small peptide (RMR) from the protein sequence of RUNX3 flanking the Threonine 209 phosphorylation site. Previous findings from our laboratory provided evidence that Threonine 209 phosphorylation of RUNX3 acts as a molecular switch in dictating the tissue-specific dualistic functions of RUNX3 for the first time. Runt-related transcription factor 3 (RUNX3) was initially known for its tumor suppressor function, but recent studies have reported the oncogenic role of RUNX3 in various cancers. P21 Activated Kinase 1 (PAK1) is an oncogenic serine/threonine kinase known to play a significant role in the regulation of cytoskeleton and cell morphology.

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