{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T15:48:04Z","timestamp":1787240884447,"version":"build-2736575974"},"reference-count":87,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"12","content-domain":{"domain":["www.science.org"],"crossmark-restriction":true},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2025,3,21]]},"abstract":"<jats:p>\n                    Centrosomes form when centrioles assemble pericentriolar material (PCM) around themselves. Spd-2\/CEP192 proteins, defined by a conserved \u201cSpd-2 domain\u201d (SP2D) comprising two closely spaced AspM-Spd-2-Hydin (ASH) domains, play a critical role in centrosome assembly. Here, we show that the SP2D does not target\n                    <jats:italic>Drosophila<\/jats:italic>\n                    Spd-2 to centrosomes but rather promotes PCM scaffold assembly. Crystal structures of the human and honeybee SP2D reveal an unusual \u201cextended cradle\u201d structure mediated by a conserved interaction interface between the two ASH domains. Mutations predicted to perturb this interface, including a human mutation associated with male infertility and Mosaic Variegated Aneuploidy, disrupt PCM scaffold assembly in flies. The SP2D is monomeric in solution, but the\n                    <jats:italic>Drosophila<\/jats:italic>\n                    SP2D can form higher-order oligomers upon phosphorylation by PLK1 (Polo-like kinase 1). Crystal-packing interactions and AlphaFold predictions suggest how SP2Ds might self-assemble, and mutations associated with one such potential dimerization interface markedly perturb SP2D oligomerization in vitro and PCM scaffold assembly in vivo.\n                  <\/jats:p>","DOI":"10.1126\/sciadv.adr5744","type":"journal-article","created":{"date-parts":[[2025,3,19]],"date-time":"2025-03-19T14:00:13Z","timestamp":1742392813000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":8,"title":["The conserved Spd-2\/CEP192 domain adopts a unique protein fold to promote centrosome scaffold assembly"],"prefix":"10.1126","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-2097-6447","authenticated-orcid":true,"given":"Liuyi","family":"Hu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, 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