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J Biol Chem. 2009 Jan 30;284(5):2902-7. doi: 10.1074/jbc.M806655200. Epub 2008 Nov 25.

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

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  • 1Institut Pasteur, Unité de Résonance Magnétique Nucleaire des Biomolécules and Unité de Biochimie Structurale et Cellulaire, CNRS, URA 2185, Paris, France. fcordier@pasteur.fr

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.

PMID:
19033441
[PubMed - indexed for MEDLINE]
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