C
Christel Brou
Researcher at Pasteur Institute
Publications - 26
Citations - 2884
Christel Brou is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Notch signaling pathway & Notch proteins. The author has an hindex of 16, co-authored 25 publications receiving 2606 citations.
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Journal ArticleDOI
A Novel Proteolytic Cleavage Involved in Notch Signaling: The Role of the Disintegrin-Metalloprotease TACE
Christel Brou,Frédérique Logeat,Neetu Gupta,Christine Bessia,Odile LeBail,John R. Doedens,Ana Cumano,Pascal Roux,Roy A. Black,Alain Israël +9 more
TL;DR: It is shown that an additional processing event occurs in the extracellular part of the receptor, preceding cleavage by the gamma-secretase-like activity, and experiments carried out on TACE-/- bone marrow-derived monocytic precursor cells suggest that this metalloprotease plays a prominent role in the activation of the Notch pathway.
Journal ArticleDOI
Delta-1 Activation of Notch-1 Signaling Results in HES-1 Transactivation
Sophie Jarriault,Odile Le Bail,Estelle Hirsinger,Olivier Pourquié,Frédérique Logeat,Clare F. Strong,Christel Brou,Nabil G. Seidah,Alain Israël +8 more
TL;DR: It is shown that vertebrate Dl-1 behaves as a functional ligand for Notch-1 and has the same ability to suppress cell differentiation as the Jagged proteins do.
Journal ArticleDOI
Monoubiquitination and endocytosis direct γ-secretase cleavage of activated Notch receptor
Neetu Gupta-Rossi,Emmanuelle Six,Odile LeBail,Frédérique Logeat,Patricia Chastagner,Annie Olry,Alain Israël,Christel Brou +7 more
TL;DR: It is demonstrated that a new modification, a monoubiquitination, as well as clathrin-dependent endocytosis, is required for γ-secretase processing of a constitutively active Notch derivative, ΔE, which mimics the TNFα-converting enzyme–processing product.
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Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains.
TL;DR: It is shown that both molecules interact and partially colocalize to endocytic vesicles, and that AIP4 targets DTX for lysosomal degradation, and polyubiquitin chains are mainly conjugated through lysine 29 of ubiquitin in vivo, indicating a link between this type of chain and lysOSomal degradation.
Journal ArticleDOI
AIP4/Itch regulates Notch receptor degradation in the absence of ligand.
TL;DR: It is demonstrated that although Notch is associated with Itch/AIP4 in cells, their interaction is not detectable in vitro and thus requires either a post-translational modification, or a bridging factor that remains to be identified.