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

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.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Blotting, Western, Cell Line, Genetic Complementation Test, Humans, Immunoprecipitation, Jurkat Cells, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Sequence Homology, Amino Acid, Ubiquitin, Zinc Fingers
J. Biol. Chem.
Date: Jan. 30, 2009
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