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

Cordier, Florence, Grubisha, Olivera ORCID: https://orcid.org/0000-0003-1067-1230, Traincard, François, Véron, Michel, Delepierre, Muriel and Agou, Fabrice 2009. The zinc finger of NEMO is a functional ubiquitin-binding domain. Journal of Biological Chemistry 284 (5) , pp. 2902-2907. 10.1074/jbc.M806655200

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Abstract

NEMO (NF-κB essential modulator) is a regulatory protein essential to the canonical NF-κB 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 η 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-κB signaling in response to tumor necrosis factor-α. Thus, our findings indicate that NEMOZFisa bona fide ubiquitin-binding domain of the ubiquitin-binding zinc finger type

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Date of First Compliant Deposit: 6 August 2018
Date of Acceptance: 19 November 2008
Last Modified: 24 Oct 2022 07:01
URI: https://orca.cardiff.ac.uk/id/eprint/113896

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