Abstract：
:RIP1 is a central mediator of cell death in response to cell stress but can also mediate cell survival by activating NF-κB. Here, we show that RIP1 acts as a switch in EGFR signaling. EGFRvIII is an oncogenic mutant that does not bind ligand and is coexpressed with EGFRWT in glioblastoma multiforme (GBM). EGFRvIII recruits ubiquitin ligases to RIP1, resulting in K63-linked ubiquitination of RIP1. RIP1 binds to TAK1 and NEMO, forming an EGFRvIII-RIP1 signalosome that activates NF-κB. RIP1 is essential for EGFRvIII-mediated oncogenicity and correlates with NF-κB activation in GBM. Surprisingly, activation of EGFRWT with EGF results in a negative regulation of EGFRvIII, with dissociation of the EGFRvIII-RIP1 signalosome, loss of RIP1 ubiquitination and NF-κB activation, and association of RIP1 with FADD and caspase-8. If EGFRWT is overexpressed with EGFRvIII, the addition of EGF leads to a RIP1 kinase-dependent cell death. The EGFRWT-EGFRvIII-RIP1 interplay may regulate oncogenicity and vulnerability to targeted treatment in GBM.
journal_name
Cell Repjournal_title
Cell reportsauthors
Puliyappadamba VT,Chakraborty S,Chauncey SS,Li L,Hatanpaa KJ,Mickey B,Noorani S,Shu HK,Burma S,Boothman DA,Habib AAdoi
10.1016/j.celrep.2013.07.025subject
Has Abstractpub_date
2013-08-29 00:00:00pages
764-75issue
4issn
2211-1247pii
S2211-1247(13)00387-2journal_volume
4pub_type
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