The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

Thibaut Eguether, Maria A. Ermolaeva, Yongge Zhao, Marion C. Bonnet, Ashish Jain, Manolis Pasparakis, Gilles Courtois and Anne-Marie Tassin ()
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Thibaut Eguether: Institut Curie/INSERM U759, Campus Universitaire
Maria A. Ermolaeva: Institute for Genetics, Center for Molecular Medicine (CMMC) and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Yongge Zhao: Laboratory of Host Defenses, NIAID, National Institutes of Health
Marion C. Bonnet: Institute for Genetics, Center for Molecular Medicine (CMMC) and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Ashish Jain: Laboratory of Host Defenses, NIAID, National Institutes of Health
Manolis Pasparakis: Institute for Genetics, Center for Molecular Medicine (CMMC) and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Gilles Courtois: Université Grenoble Alpes
Anne-Marie Tassin: Institut Curie/INSERM U759, Campus Universitaire

Nature Communications, 2014, vol. 5, issue 1, 1-14

Abstract: Abstract CYLD is a tumour suppressor gene mutated in familial cylindromatosis, a genetic disorder leading to the development of skin appendage tumours. It encodes a deubiquitinating enzyme that removes Lys63- or linear-linked ubiquitin chains. CYLD was shown to regulate cell proliferation, cell survival and inflammatory responses, through various signalling pathways. Here we show that CYLD localizes at centrosomes and basal bodies via interaction with the centrosomal protein CAP350 and demonstrate that CYLD must be both at the centrosome and catalytically active to promote ciliogenesis independently of NF-κB. In transgenic mice engineered to mimic the smallest truncation found in cylindromatosis patients, CYLD interaction with CAP350 is lost disrupting CYLD centrosome localization, which results in cilia formation defects due to impairment of basal body migration and docking. These results point to an undiscovered regulation of ciliogenesis by Lys63 ubiquitination and provide new perspectives regarding CYLD function that should be considered in the context of cylindromatosis.

Date: 2014
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DOI: 10.1038/ncomms5585

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