%0 Journal Article %T CYLD Regulates Centriolar Satellites Proteostasis by Counteracting the E3 Ligase MIB1 %+ Signaling in Oncogenesis, Angiogenesis and Permeability (CRCINA-ÉQUIPE 15) %+ Institut de Cancérologie de l'Ouest [Angers/Nantes] (UNICANCER/ICO) %A Douanne, Tiphaine %A André-Grégoire, Gwennan %A Thys, An %A Trillet, Kilian %A Gavard, Julie %A Bidère, Nicolas %Z This research was funded by an International Program for Scientific Cooperation (PICS, CNRS), Fondation ARC pour la recherche sur le Cancer (N.B.), Ligue nationale contre le cancer comités de Loire-Atlantique, Maine et Loire, Vendée (J.G., N.B.), Région Pays de la Loire et Nantes Métropole under Connect Talent Grant (J.G.), the National Research Agency under the Programme d’Investissements d’Avenir (ANR-16-IDEX-0007), and the SIRIC ILIAD (INCa-DGOS-Inserm_12558). T.D. is a PhD fellow funded by Nantes Métropole and G.A.G. and A.T. hold postdoctoral fellowships from Fondation de France and Fondation ARC, respectively. Team projects are funded by Equipe Labellisée Fondation pour la Recherche Médicale (FRM DEQ20180339184). %< avec comité de lecture %@ 2211-1247 %J Cell Reports %I Elsevier Inc %V 27 %N 6 %P 1657-1665 %8 2019-05-07 %D 2019 %R 10.1016/j.celrep.2019.04.036 %M 31067453 %K centriolar satellites %K PCM1 %K CYLD %K ciliogenesis %K proteostasis %K ubiquitin %K MIB1 %Z Life Sciences [q-bio]/Cellular BiologyJournal articles %X The tumor suppressor CYLD is a deubiquitinating enzyme that removes non-degradative ubiquitin linkages bound to a variety of signal transduction adaptors. CYLD participates in the formation of primary cilia, a microtubule-based structure that protrudes from the cell body to act as a "sensing antenna." Yet, how exactly CYLD regulates ciliogenesis is not fully understood. Here, we conducted an unbiased proteomic screen of CYLD binding partners and identified components of the centriolar satellites. These small granular structures, tethered to the scaffold protein pericentriolar matrix protein 1 (PCM1), gravitate toward the centrosome and orchestrate ciliogenesis. CYLD knockdown promotes PCM1 degradation and the subsequent dismantling of the centriolar satellites. We found that CYLD marshals the centriolar satellites by deubiquitinating and preventing the E3 ligase Mindbomb 1 (MIB1) from marking PCM1 for proteasomal degradation. These results link CYLD to the regulation of centriolar satellites proteostasis and provide insight into how reversible ubiquitination finely tunes ciliogenesis. %G English %2 https://inserm.hal.science/inserm-02128157/document %2 https://inserm.hal.science/inserm-02128157/file/mmc2-1.pdf %L inserm-02128157 %U https://inserm.hal.science/inserm-02128157 %~ INSERM %~ UNIV-NANTES %~ CNRS %~ UNIV-ANGERS %~ CRCINA %~ ANR %~ NANTES-UNIVERSITE %~ UNIV-NANTES-AV2022 %~ FRM