KCIP-1 Protein, Mouse (P.pastoris, His, solution)

TRADD functions as an adapter molecule for TNFRSF1A/TNFR1, forming a complex with the activated TNFRSF1A/TNFR1 and mediating its interaction with FADD. Overexpression of TRADD induces two major TNF-induced responses: apoptosis and activation of NF-kappa-B. The nuclear form of TRADD acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A through interaction with TRIP12, disrupting the interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A. Stimulation of TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I, composed of TNFRSF1A, TRADD, RIPK1, TRAF2, and BIRC2/c-IAP1 or BIRC3, interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta, and IKBKG/IKK-gamma, promoting cell survival. Subsequently, TRADD, RIPK1, and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8, promoting cell apoptosis. TRADD interacts with various proteins within complex I, including TNFRSF1A/TNFR1, TRAF2, kinase RIPK1, TRPC4AP, and scaffold protein DAB2IP. It also interacts with autophagy receptor SQSTM1, E3 ligase TRIP12, kinase HIPK2, and keratins KRT14, KRT18, KRT16, and KRT17. Additionally, TRADD interacts with TOMM70.