Cellular Inhibitors of Apoptosis Are Global Regulators of NF-κB and MAPK Activation by Members of the TNF Family of Receptors

Eugene Varfolomeev, Tatiana Goncharov, Heather Maecker, Kerry Zobel, László G. Kömüves, Kurt Deshayes, Domagoj Vucic*

*To whom correspondence should be addressed. E-mail: domagoj{at}gene.com

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• Materials and Methods
• Fig. S1. Characterization of commercial antibodies against c-IAP1, c-IAP2, TRAF2, TRAF3, TRAF6, IKK2, NEMO, TAK1, and HOIP.
• Fig. S2. Characterization of the cell surface expression of members of the TNFR family.
• Fig. S3. c-IAPs are required for canonical NF-κB, JNK, and p38 activation by TNF-α, TWEAK, LIGHT, CD27L, and CD30L.
• Fig. S4. TRAF6 and c-IAP proteins mediate CD40-dependent activation of the canonical NF-κB pathway.
• Fig. S5. TNF-α–, TWEAK-, and LIGHT-stimulated NF-κB and JNK activation depends on c-IAP1 and c-IAP2.
• Fig. S6. Loss of c-IAP proteins results in reduced expression of genes regulated by members of the TNF family.
• Fig. S7. c-IAP proteins regulate the function of complexes involving TNFR family members.
• Fig. S8. TNF-α–, TWEAK-, and LIGHT-stimulated NF-κB and JNK activation depends on NEMO and HOIP.
• Fig. S9. Differential effects of the signaling of TNFR family members on the stability of c-IAP1, c-IAP2, TRAF2, and TRAF3 proteins.
• Fig. S10. Proteasome and lysosome inhibitors stabilize c-IAP and TRAF proteins during signaling by TNF family members.
• Fig. S11. Membrane targeting of TRAF2 or c-IAP1 reduces their cytoplasmic abundance and enables noncanonical NF-κB signaling.
• Fig. S12. BR3 signaling triggers the translocation of TRAF3 to the insoluble fraction.
  

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© 2012 American Association for the Advancement of Science