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.
Pubmed ID: 31067453 RIS Download
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View all literature mentionsDatabase of known and predicted protein interactions. The interactions include direct (physical) and indirect (functional) associations and are derived from four sources: Genomic Context, High-throughput experiments, (Conserved) Coexpression, and previous knowledge. STRING quantitatively integrates interaction data from these sources for a large number of organisms, and transfers information between these organisms where applicable. The database currently covers 5''214''234 proteins from 1133 organisms. (2013)
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