Cell Reports volume 4, issue 4, P764-775 2013 DOI: 10.1016/j.celrep.2013.07.025 View full text
Vineshkumar Thidil Puliyappadamba, Sharmistha Chakraborty, Sandili S. Chauncey, Li Li, Kimmo J. Hatanpaa, Bruce Mickey, Shayan Noorani, Hui-Kuo G. Shu, Sandeep Burma, David A. Boothman, Amyn A. Habib

Abstract: Summary RIP1 is a central mediator of cell death in cell stress, but can also mediate cell survival by activating NF-κB. Here, we show that RIP1 is a switch in EGFR signaling. EGFRvIII is an oncogenic mutant that does not bind ligand and is co-expressed with EGFRwt in glioblastoma (GBM). EGFRvIII recruits ubiquitin ligases to RIP1 resulting in K63-linked ubiquitination of RIP1. RIP1 binds to TAK1 and NEMO forming a EGFRvIII-RIP1 signalosome that activates NF-κB. RIP1 is essential for EGFRvIII-mediated oncogen…

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