Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/s41467-018-04431-1
Keywords
-
Categories
Funding
- Ligue Nationale Contre le Cancer [INCa PLBio 2016-161, ANR-16-CE11-0032-04]
- French Proteomic Infrastructure (ProFI) [ANR-10-INBS-08-03]
- GIS IBiSA
- Region Alsace
- FCT-Fundacao para a Ciencia e a Tecnologia [PTDC/BBB-BEP/1463/2014]
- FEDER
- Fundacao para a Ciencia e Tecnologia/Ministerio da Educacao e Ciencia [iNOVA4Health - UID/Multi/04462/2013]
- Ligue Nationale Contre le Cancer
- [SFRH/BD/111603/2015]
Ask authors/readers for more resources
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-alpha 2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha 2 expression and for the assembly of liprin-alpha 2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available