دورية أكاديمية

CYLD Regulates Centriolar Satellites Proteostasis by Counteracting the E3 Ligase MIB1

التفاصيل البيبلوغرافية
العنوان: CYLD Regulates Centriolar Satellites Proteostasis by Counteracting the E3 Ligase MIB1
المؤلفون: Douanne, Tiphaine, André-Grégoire, Gwennan, Thys, An, Trillet, Kilian, Gavard, Julie, Bidère, Nicolas
المساهمون: Signaling in Oncogenesis, Angiogenesis and Permeability (CRCINA-ÉQUIPE 15), Centre de Recherche en Cancérologie et Immunologie Nantes-Angers (CRCINA), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Universitaire de Nantes = Nantes University Hospital (CHU Nantes)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Universitaire de Nantes = Nantes University Hospital (CHU Nantes)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), Institut de Cancérologie de l'Ouest Angers/Nantes (UNICANCER/ICO), UNICANCER, 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)., ANR-16-IDEX-0007,NExT (I-SITE),NExT (I-SITE)(2016)
المصدر: ISSN: 2211-1247.
بيانات النشر: HAL CCSD
Elsevier Inc
سنة النشر: 2019
المجموعة: Université de Nantes: HAL-UNIV-NANTES
مصطلحات موضوعية: centriolar satellites, PCM1, CYLD, ciliogenesis, proteostasis, ubiquitin, MIB1, [SDV.BC]Life Sciences [q-bio]/Cellular Biology
الوصف: International audience ; 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.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/31067453; inserm-02128157; https://inserm.hal.science/inserm-02128157Test; https://inserm.hal.science/inserm-02128157/documentTest; https://inserm.hal.science/inserm-02128157/file/mmc2-1.pdfTest; PUBMED: 31067453
DOI: 10.1016/j.celrep.2019.04.036
الإتاحة: https://doi.org/10.1016/j.celrep.2019.04.036Test
https://inserm.hal.science/inserm-02128157Test
https://inserm.hal.science/inserm-02128157/documentTest
https://inserm.hal.science/inserm-02128157/file/mmc2-1.pdfTest
حقوق: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.ED38B73
قاعدة البيانات: BASE