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Zfra affects TNF-mediated cell death by interacting with death domain protein TRADD and negatively regulates the activation of NF-κB, JNK1, p53 and WOX1 during stress response-6

By Qunying Hong (76030), Li-Jin Hsu (76031), Lori Schultz (76032), Nicole Pratt (76033), Jeffrey Mattison (76034) and Nan-Shan Chang (76035)

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Zfra affects TNF-mediated cell death by interacting with death domain protein TRADD and negatively regulates the activation of NF-κB, JNK1, p53 and WOX1 during stress response"</p><p>http://www.biomedcentral.com/1471-2199/8/50</p><p>BMC Molecular Biology 2007;8():50-50.</p><p>Published online 13 Jun 2007</p><p>PMCID:PMC1904229.</p><p></p>ased the binding of GST-Zfra with NF-κB (p65) and JNK1 (greater than 50%), and weakly with p53 but not IκBα. GST-Zfra physically interacted with endogenous Zfra and WOX1, and TNF limitedly increased the binding (less than 30%). In negative controls, GST alone could not bind the above-indicated proteins. The relative amounts of GST and GST-Zfra used in the pull down are shown. One-twentieth amounts of protein input for endogenous Zfra and other indicated proteins are shown in Western blotting. () Similarly, during a 10-min treatment, TNF increased the binding of GST-Zfra with p-WOX1, but not with FADD, RIP, IκBα and Fas. () SK-N-SH cells were exposed to UV light (120 mJoule/cm) and then cultured for 1 hr, followed by processing GST pull-down analysis. UV light increased the binding of endogenous Zfra with p-WOX1 and JNK1. () By co-immunoprecipitation, UV light (120 mJoule/cm) increased the binding of endogenous Zfra with itself and p-JNK1 (at Thr183/Tyr185) (greater than 50% increase), but limitedly with WOX1 (less than 20% increase), in SK-N-SH cells

Topics: Molecular Biology, zfra, nfb, activation, regulates, negatively, tradd, protein, domain, interacting, death, cell, tnfmediated, affects, stress
Year: 2011
DOI identifier: 10.6084/m9.figshare.57918.v1
OAI identifier: oai:figshare.com:article/57918
Provided by: FigShare
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