F
Fabrice Agou
Researcher at Pasteur Institute
Publications - 40
Citations - 2644
Fabrice Agou is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Ubiquitin binding & IκB kinase. The author has an hindex of 18, co-authored 35 publications receiving 2439 citations.
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Journal ArticleDOI
Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation
Shoji Yamaoka,Gilles Courtois,Christine Bessia,Simon T. Whiteside,Robert Weil,Fabrice Agou,Heather Kirk,Robert J. Kay,Alain Israël +8 more
TL;DR: A flat cellular variant of HTLV-1 Tax-transformed rat fibroblasts, 5R, which is unresponsive to all tested NF-κB activating stimuli is characterized, and its genetic complementation is reported.
Journal ArticleDOI
Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency
Bertrand Boisson,Emmanuel Laplantine,Carolina Prando,Silvia Giliani,Elisabeth Israelsson,Zhaohui Xu,Avinash Abhyankar,Laura Israel,Laura Israel,Giraldina Trevejo-Nunez,Dusan Bogunovic,Alma-Martina Cepika,Donna A. MacDuff,Maya Chrabieh,Maya Chrabieh,Marjorie Hubeau,Marjorie Hubeau,Fanny Bajolle,Marianne Debré,Evelina Mazzolari,Donatella Vairo,Fabrice Agou,Herbert W. Virgin,Xavier Bossuyt,Caroline Rambaud,Fabio Facchetti,Damien Bonnet,Damien Bonnet,Pierre Quartier,Pierre Quartier,Jean-Christophe Fournet,Jean-Christophe Fournet,Virginia Pascual,Damien Chaussabel,Damien Chaussabel,Luigi D. Notarangelo,Anne Puel,Anne Puel,Alain Israël,Jean-Laurent Casanova,Capucine Picard +40 more
TL;DR: It is suggested that LUBAC regulates NF-κB–dependent IL-1β responses differently in different cell types, consistent with the unique association of autoinflammation and immunodeficiency in patients from two kindreds.
Journal ArticleDOI
NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
Emmanuel Laplantine,Elisabeth Fontan,Jeanne Chiaravalli,T Lopez,G Lakisic,Michel Véron,Fabrice Agou,Alain Israël +7 more
TL;DR: It is demonstrated that together they form a bipartite high‐affinity K63‐specific ubiquitin‐binding domain, which suggests that the main function of the C‐terminal half of NEMO is to specifically bind K 63‐linked poly‐ubiquitin chains.
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NEMO trimerizes through its coiled-coil C-terminal domain.
Fabrice Agou,Fei Ye,Stéphane Goffinont,Gilles Courtois,Shoji Yamaoka,Alain Israël,Michel Véron +6 more
TL;DR: In vivo cross-linking experiments indicate that native N EMO in association with IKK is in equilibrium between a dimeric and a trimeric form, suggesting that the association of NEMO with Ikk or with Hsp70 prevents incorrect interdomain pairing reactions that could lead to aggregation or to an non-native oligomeric state of rNEMO.
Journal ArticleDOI
The Zinc Finger of NEMO Is a Functional Ubiquitin-binding Domain
Florence Cordier,Olivera Grubisha,François Traincard,Michel Véron,Muriel Delepierre,Fabrice Agou +5 more
TL;DR: 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.