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The zinc finger of NEMO is a functional ubiquitin-binding domain.

Abstract : NEMO (NF-kappaB essential modulator) is a regulatory protein essential to the canonical NF-kappaB signaling pathway, notably involved in immune and inflammatory responses, apoptosis, and oncogenesis. Here, we report that the zinc finger (ZF) motif, located in the regulatory C-terminal half of NEMO, forms a specific complex with ubiquitin. We have investigated the NEMO ZF-ubiquitin interaction and proposed a structural model of the complex based on NMR, fluorescence, and mutagenesis data and on the sequence homology with the polymerase eta ubiquitin-binding zinc finger involved in DNA repair. Functional complementation assays and in vivo pull-down experiments further show that ZF residues involved in ubiquitin binding are functionally important and required for NF-kappaB signaling in response to tumor necrosis factor-alpha. Thus, our findings indicate that NEMOZFisa bona fide ubiquitin-binding domain of the ubiquitin-binding zinc finger type.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-00366746
Contributor : Cécile Roux <>
Submitted on : Monday, March 9, 2009 - 3:48:38 PM
Last modification on : Wednesday, May 6, 2020 - 8:46:03 PM

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Florence Cordier, Olivera Grubisha, François Traincard, Michel Véron, Muriel Delepierre, et al.. The zinc finger of NEMO is a functional ubiquitin-binding domain.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (5), pp.2902-7. ⟨10.1074/jbc.M806655200⟩. ⟨pasteur-00366746⟩

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