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Here, we identify a role for the mammalian homologue of yeast SFI1, involved in the duplication of the yeast spindle pole body, as a critical regulator of centriole duplication in mammalian cells. Mammalian SFI1 interacts with USP9X, a deubiquitylase associated with human syndromic mental retardation. SFI1 localizes USP9X to the centrosome during S phase to deubiquitylate STIL, a critical regulator of centriole duplication. USP9X-mediated deubiquitylation protects STIL from degradation. Consistent with a role for USP9X in stabilizing STIL, cells from patients with USP9X loss-of-function mutations have reduced STIL levels. Together, these results demonstrate that SFI1 is a centrosomal protein that localizes USP9X to the centrosome to stabilize STIL and promote centriole duplication. We propose that the USP9X protection of STIL to facilitate centriole duplication underlies roles of both proteins in human neurodevelopment.<\/jats:p>","DOI":"10.1083\/jcb.201803041","type":"journal-article","created":{"date-parts":[[2019,6,13]],"date-time":"2019-06-13T18:25:14Z","timestamp":1560450314000},"page":"2185-2197","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":24,"title":["SFI1 promotes centriole duplication by recruiting USP9X to stabilize the microcephaly protein STIL"],"prefix":"10.1083","volume":"218","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9662-0615","authenticated-orcid":true,"given":"Andrew","family":"Kodani","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 1"},{"name":"Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 2"},{"name":"Division of Genetics and Genomics and Howard Hughes Medical Institute, Boston Children\u2019s Hospital, Boston, MA 4"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tyler","family":"Moyer","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 3"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Allen","family":"Chen","sequence":"additional","affiliation":[{"name":"Division of Genetics and Genomics and Howard Hughes Medical Institute, Boston Children\u2019s Hospital, Boston, MA 4"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3728-6367","authenticated-orcid":true,"given":"Andrew","family":"Holland","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 3"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher A.","family":"Walsh","sequence":"additional","affiliation":[{"name":"Division of Genetics and Genomics and Howard Hughes Medical Institute, Boston Children\u2019s Hospital, Boston, MA 4"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeremy F.","family":"Reiter","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 1"},{"name":"Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 2"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[2019,6,13]]},"reference":[{"key":"2023072310065727700_bib1","doi-asserted-by":"crossref","first-page":"4233","DOI":"10.1074\/mcp.M111.014233","article-title":"Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture","volume":"11","author":"Al-Hakim","year":"2012","journal-title":"Mol. 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