Journal
CELL REPORTS
Volume 27, Issue 6, Pages 1657-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2019.04.036
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Funding
- International Program for Scientific Cooperation (PICS, CNRS)
- Fondation ARC pour la recherche sur le Cancer
- Ligue nationale contre le cancer comites de Loire-Atlantique, Maine et Loire, Vendee
- Region Pays de la Loire et Nantes Metropole under Connect Talent Grant
- National Research Agency under the Programme d'Investissements d'Avenir [ANR-16-IDEX-0007]
- SIRIC ILIAD [INCa-DGOS-Inserm_12558]
- Nantes Metropole
- Fondation de France
- Fondation ARC
- Equipe Labellisee Fondation pour la Recherche Medicale [FRM DEQ20180339184]
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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.
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