The Zinc Finger of NEMO Is a Functional Ubiquitin-binding Domain
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...
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| Veröffentlicht in: | The Journal of biological chemistry 2009-01, Vol.284 (5), p.2902-2907 |
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| creator | Cordier, Florence Grubisha, Olivera Traincard, François Véron, Michel Delepierre, Muriel Agou, Fabrice |
| description | 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. |
| doi_str_mv | 10.1074/jbc.M806655200 |
| format | Article |
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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. 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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. 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| subjects | Amino Acid Sequence Binding Sites Biochemistry, Molecular Biology Blotting, Western Cell Line Genetic Complementation Test Humans Immunoprecipitation Jurkat Cells Life Sciences Models, Molecular Nuclear Magnetic Resonance, Biomolecular Sequence Homology, Amino Acid Structural Biology Ubiquitin - chemistry Ubiquitin - metabolism Zinc Fingers |
| title | The Zinc Finger of NEMO Is a Functional Ubiquitin-binding Domain |
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