Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates
The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB path...
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| Vydáno v: | Nature communications Ročník 15; číslo 1; s. 7692 - 19 |
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| Hlavní autoři: | , , , , , , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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Nature Publishing Group UK
03.09.2024
Nature Publishing Group Springer Science and Business Media LLC Nature Portfolio |
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| ISSN: | 2041-1723, 2041-1723 |
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| Abstract | The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif’s conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition.
The inhibitor of kB kinase (IKK) is a central regulator of NF-kB signalling. Here the authors identify a motif conserved in substrates of canonical and alternative NF-kB pathways which mediates docking to catalytic IKK dimers: they show that phosphorylation of the conserved tyrosine suppresses the docking interaction. |
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| AbstractList | The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif's conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition. The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif’s conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition. The inhibitor of kB kinase (IKK) is a central regulator of NF-kB signalling. Here the authors identify a motif conserved in substrates of canonical and alternative NF-kB pathways which mediates docking to catalytic IKK dimers: they show that phosphorylation of the conserved tyrosine suppresses the docking interaction. The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif’s conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition. The inhibitor of kB kinase (IKK) is a central regulator of NF-kB signalling. Here the authors identify a motif conserved in substrates of canonical and alternative NF-kB pathways which mediates docking to catalytic IKK dimers: they show that phosphorylation of the conserved tyrosine suppresses the docking interaction. The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif's conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition.The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif's conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition. Abstract The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif’s conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition. The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero-or homodimers of the catalytic IKKβ and/or IKKα subunits. Here, we identify a YDDΦxΦ motif, which is conserved in substrates of canonical (IκBα, IκBβ) and alternative (p100) NF-κB pathways, and which mediates docking to catalytic IKK dimers. We demonstrate a quantitative correlation between docking affinity and IKK activity related to IκBα phosphorylation/degradation. Furthermore, we show that phosphorylation of the motif's conserved tyrosine, an event previously reported to promote IκBα accumulation and inhibition of NF-κB gene expression, suppresses the docking interaction. Results from integrated structural analyzes indicate that the motif binds to a groove at the IKK dimer interface. Consistently, suppression of IKK dimerization also abolishes IκBα substrate binding. Finally, we show that an optimized bivalent motif peptide inhibits NF-κB signaling. This work unveils a function for IKKα/β dimerization in substrate motif recognition.Nuclear factor κB (NF-κB) signaling plays a central role in the regulation of cellular inflammatory, immune, and apoptotic responses 1 . Under homeostatic conditions, NF-κB dimers are sequestered in the cytoplasm by interaction with inhibitor of κB (IκB) proteins or with the NF-κB precursor proteins p100 and p105. Receptor stimulation of the 'canonical' NF-κB pathway activates the inhibitor of κB (IκB) kinase (IKK), which, in turn, phosphorylates IκB proteins. This results in the ubiquitin-mediated degradation of IκB and subsequent nuclear translocation of p65/p50 NF-κB dimers 2 . Stimulation of the 'alternative' NF-κB pathway leads instead to IKK-mediated phosphorylation of p100, which triggers partial degradation of p100 into the mature p52 NF-κB subunit 2 .Different IKK complexes (collectively referred to as IKKs hereafter) exist in cells and exhibit variable subunit composition. The core of the canonical IKK complex comprises a heterodimer of the catalytic IKKα/1 and IKKβ/2 subunits (named IKKα and IKKβ hereafter) and two copies of the regulatory NEMO subunit 3-5 . Whereas IKKα contributes to kinase activation by phosphorylating the IKKβ activation loop 6 , the IKKβ subunit directly phosphorylates a phospho-dependent D p SGxx p S/T βTrCP degron motif (where pS or pT are phosphoserine |
| ArticleNumber | 7692 |
| Author | McEwen, Alastair G. Li, Changqing Donzeau, Mariel Shostak, Kateryna Rappsilber, Juri Orfanoudakis, Georges Graziadei, Andrea Fiskin, Mert Davey, Norman E. Moro, Stefano Poterszman, Arnaud Torbeev, Vladimir Bachelart, Thomas Pichard, Simon Zanier, Katia Berrodier, Nicolas O’Reilly, Francis J. Chariot, Alain Desplancq, Dominique Poussin-Courmontagne, Pierre Brillet, Karl |
| Author_xml | – sequence: 1 givenname: Changqing surname: Li fullname: Li, Changqing organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 2 givenname: Stefano surname: Moro fullname: Moro, Stefano organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 3 givenname: Kateryna orcidid: 0000-0002-9946-3536 surname: Shostak fullname: Shostak, Kateryna organization: Laboratory of Cancer Biology, GIGA Cancer, University of Liege, CHU – sequence: 4 givenname: Francis J. orcidid: 0000-0001-9258-0150 surname: O’Reilly fullname: O’Reilly, Francis J. organization: Institute of Biotechnology, Technische Universität Berlin – sequence: 5 givenname: Mariel surname: Donzeau fullname: Donzeau, Mariel organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 6 givenname: Andrea surname: Graziadei fullname: Graziadei, Andrea organization: Institute of Biotechnology, Technische Universität Berlin – sequence: 7 givenname: Alastair G. orcidid: 0000-0003-4484-3512 surname: McEwen fullname: McEwen, Alastair G. organization: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) / INSERM UMR-S 1258 / CNRS UMR7104/ Université de Strasbourg – sequence: 8 givenname: Dominique surname: Desplancq fullname: Desplancq, Dominique organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 9 givenname: Pierre orcidid: 0000-0003-4813-6882 surname: Poussin-Courmontagne fullname: Poussin-Courmontagne, Pierre organization: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) / INSERM UMR-S 1258 / CNRS UMR7104/ Université de Strasbourg – sequence: 10 givenname: Thomas surname: Bachelart fullname: Bachelart, Thomas organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 11 givenname: Mert surname: Fiskin fullname: Fiskin, Mert organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 12 givenname: Nicolas surname: Berrodier fullname: Berrodier, Nicolas organization: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) / INSERM UMR-S 1258 / CNRS UMR7104/ Université de Strasbourg – sequence: 13 givenname: Simon orcidid: 0009-0008-9765-4006 surname: Pichard fullname: Pichard, Simon organization: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) / INSERM UMR-S 1258 / CNRS UMR7104/ Université de Strasbourg – sequence: 14 givenname: Karl orcidid: 0000-0002-7900-8923 surname: Brillet fullname: Brillet, Karl organization: Institut Biologie Moléculaire et Cellulaire (IBMC), CNRS UPR9002 – sequence: 15 givenname: Georges surname: Orfanoudakis fullname: Orfanoudakis, Georges organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 16 givenname: Arnaud orcidid: 0000-0002-6702-5777 surname: Poterszman fullname: Poterszman, Arnaud organization: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) / INSERM UMR-S 1258 / CNRS UMR7104/ Université de Strasbourg – sequence: 17 givenname: Vladimir surname: Torbeev fullname: Torbeev, Vladimir organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant – sequence: 18 givenname: Juri orcidid: 0000-0001-5999-1310 surname: Rappsilber fullname: Rappsilber, Juri organization: Institute of Biotechnology, Technische Universität Berlin – sequence: 19 givenname: Norman E. surname: Davey fullname: Davey, Norman E. organization: Division of Cancer Biology, The Institute of Cancer Research – sequence: 20 givenname: Alain surname: Chariot fullname: Chariot, Alain organization: Laboratory of Cancer Biology, GIGA Cancer, University of Liege, CHU, WELBIO department, WEL Research Institute – sequence: 21 givenname: Katia orcidid: 0000-0002-7183-7356 surname: Zanier fullname: Zanier, Katia email: zanier@unistra.fr organization: Biotechnology and Cell Signaling (CNRS/Université de Strasbourg, UMR7242), Ecole Superieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant |
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| DOI | 10.1038/s41467-024-52076-0 |
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| Snippet | The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or... The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero-or homodimers of the catalytic IKKβ and/or... Abstract The inhibitor of κB (IκB) kinase (IKK) is a central regulator of NF-κB signaling. All IKK complexes contain hetero- or homodimers of the catalytic... |
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| Title | Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates |
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