The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones

Chloé Maurizy, Marc Quinternet, Yoann Abel, Céline Verheggen, Paulo E. Santo, Maxime Bourguet, Ana C.F. Paiva, Benoît Bragantini, Marie-Eve Chagot, Marie-Cécile Robert, Claire Abeza, Philippe Fabre, Philippe Fort, Franck Vandermoere, Pedro M.F. Sousa, Jean-Christophe Rain, Bruno Charpentier, Sarah Cianférani, Tiago M. Bandeiras, Bérengère Pradet-Balade, Xavier Manival () and Edouard Bertrand ()
Additional contact information
Chloé Maurizy: Université de Montpellier
Marc Quinternet: Université de Lorraine
Yoann Abel: Université de Montpellier
Céline Verheggen: Université de Montpellier
Paulo E. Santo: Instituto de Biologia Experimental e Tecnológica
Maxime Bourguet: Université de Strasbourg
Ana C.F. Paiva: Instituto de Biologia Experimental e Tecnológica
Benoît Bragantini: Université de Lorraine
Marie-Eve Chagot: Université de Lorraine
Marie-Cécile Robert: Université de Montpellier
Claire Abeza: Université de Montpellier
Philippe Fabre: Université de Lorraine
Philippe Fort: University of Montpellier, CNRS
Franck Vandermoere: Université de Montpellier
Pedro M.F. Sousa: Instituto de Biologia Experimental e Tecnológica
Jean-Christophe Rain: Hybrigenics Services
Bruno Charpentier: Université de Lorraine
Sarah Cianférani: Université de Strasbourg
Tiago M. Bandeiras: Instituto de Biologia Experimental e Tecnológica
Bérengère Pradet-Balade: University of Montpellier, CNRS
Xavier Manival: Université de Lorraine
Edouard Bertrand: Université de Montpellier

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: Abstract R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an 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-α2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-α2 expression and for the assembly of liprin-α2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 °C, suggesting that R2SP could help compensating the lower temperate of testis.

Date: 2018
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DOI: 10.1038/s41467-018-04431-1

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