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- W2938261111 abstract "Abstract Centrosomal protein 120 (CEP120) was originally identified as a daughter centriole-enriched protein that participates in centriole elongation. Recent studies showed that CEP120 gene mutations cause complex ciliopathy phenotypes in humans, including Joubert syndrome and Jeune asphyxiating thoracic dystrophy, suggesting that CEP120 plays an additional role in ciliogenesis. To investigate the potential roles of CEP120 in centriole elongation and cilia formation, we knocked out the CEP120 gene in p53-deficient RPE1 cells using the CRISPR/Cas9 editing system, and performed various analyses. We herein report that loss of CEP120 produces short centrioles with no apparent distal and subdistal appendages. CEP120 knockout was also associated with defective centriole elongation, impaired recruitment of C2CD3 and Talpid3 to the distal ends of centrioles, and consequent defects in centriole appendage assembly and cilia formation. Interestingly, wild-type CEP120 interacts with C2CD3 and Talpid3, whereas a disease-associated CEP120 mutant (I975S) has a low affinity for C2CD3 binding and perturbs cilia assembly. Together, our findings reveal a novel role of CEP120 in ciliogenesis by showing that it interacts with C2CD3 and Talpid3 to assemble centriole appendages and by illuminating the molecular mechanism through which the CEP120 (I975S) mutation causes complex ciliopathies." @default.
- W2938261111 created "2019-04-25" @default.
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- W2938261111 date "2019-04-15" @default.
- W2938261111 modified "2023-10-09" @default.
- W2938261111 title "CEP120 interacts with C2CD3 and Talpid3 and is required for centriole appendage assembly and ciliogenesis" @default.
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- W2938261111 doi "https://doi.org/10.1038/s41598-019-42577-0" @default.
- W2938261111 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6465297" @default.
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