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Inactivation of assembly often causes cilia defects and underlies ciliopathy, while diseases caused by dysfunction in disassembly remain largely unknown. Here, we demonstrate that CEP55 functions as a cilia disassembly regulator to participate in ciliopathy. Cep55\u2212\/\u2212 mice display clinical manifestations of Meckel\u2013Gruber syndrome, including perinatal death, polycystic kidneys, and abnormalities in the CNS. Interestingly, Cep55\u2212\/\u2212 mice exhibit an abnormal elongation of cilia on these tissues. Mechanistically, CEP55 promotes cilia disassembly by interacting with and stabilizing Aurora A kinase, which is achieved through facilitating the chaperonin CCT complex to Aurora A. In addition, CEP55 mutation in Meckel\u2013Gruber syndrome causes the failure of cilia disassembly. Thus, our study establishes a cilia disassembly role for CEP55 in vivo, coupling defects in cilia disassembly to ciliopathy and further suggesting that proper cilia dynamics are critical for mammalian development.<\/jats:p>","DOI":"10.1083\/jcb.202003149","type":"journal-article","created":{"date-parts":[[2021,1,21]],"date-time":"2021-01-21T14:39:27Z","timestamp":1611239967000},"update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":30,"title":["CEP55 promotes cilia disassembly through stabilizing Aurora A kinase"],"prefix":"10.1083","volume":"220","author":[{"given":"Yu-Cheng","family":"Zhang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Proteomics, National Center of Biomedical Analysis, Beijing, China 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yun-Feng","family":"Bai","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Proteomics, National Center of Biomedical 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