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It is composed of\u00a0an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1\/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1\/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1\/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-\u03b12, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-\u03b12 expression and for the assembly of liprin-\u03b12 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32\u2009\u00b0C, suggesting that R2SP could help compensating the lower temperate of testis.<\/jats:p>","DOI":"10.1038\/s41467-018-04431-1","type":"journal-article","created":{"date-parts":[[2018,5,22]],"date-time":"2018-05-22T10:15:52Z","timestamp":1526984152000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":77,"title":["The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones"],"prefix":"10.1038","volume":"9","author":[{"given":"Chlo\u00e9","family":"Maurizy","sequence":"first","affiliation":[]},{"given":"Marc","family":"Quinternet","sequence":"additional","affiliation":[]},{"given":"Yoann","family":"Abel","sequence":"additional","affiliation":[]},{"given":"C\u00e9line","family":"Verheggen","sequence":"additional","affiliation":[]},{"given":"Paulo E.","family":"Santo","sequence":"additional","affiliation":[]},{"given":"Maxime","family":"Bourguet","sequence":"additional","affiliation":[]},{"given":"Ana","family":"C.F. 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