ArticleNature communications2018
The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 81 citations in OpenAlex.
- DNAAF19-RUVBL1/2 complex recruits multiple adaptors to promote dynein arm assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.The Journal of biological chemistry · 2026Review
- Rearrangement of the Cell Chaperone Machinery in Human Fibrosarcoma HT1080 Cells With the Knocked-Out HSP90AA1 Gene Encoding Hsp90α.Biology of the cell · 2026Article
- An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex.Nature communications · 2026Article
- Co-translational determination of quaternary structures in chaperone factories.Nature communications · 2026Article
- DynAPs and cytoplasmic assembly of axonemal dyneins.Journal of cell science · 2025Article
- RuvBL1/2 reduce toxic dipeptide repeat protein burden in multiple models of C9orf72-ALS/FTD.Life science alliance · 2025Article
- The nucleolar phase of signal recognition particle assembly.Life science alliance · 2024Article
- Denaturing mass photometry for rapid optimization of chemical protein-protein cross-linking reactions.Nature communications · 2024Article
- DIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes.Nature methods · 2024Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- Article
- Maturation and Assembly of mTOR Complexes by the HSP90-R2TP-TTT Chaperone System: Molecular Insights and Mechanisms.Sub-cellular biochemistry · 2024Review
- Article
- Proteomic analyses reveal new features of the box H/ACA RNP biogenesis.Nucleic acids research · 2023Article
- Clinicopathological Significances and Prognostic Value ofJournal of Cancer · 2023Article
- Riluzole partially restores RNA polymerase III complex assembly in cells expressing the leukodystrophy-causative variant POLR3B R103H.Molecular brain · 2022Article
- FBB18 participates in preassembly of almost all axonemal dyneins independent of R2TP complex.PLoS genetics · 2022Article
- The Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization.Biomolecules · 2022Review
- The role of SPAG1 in the assembly of axonemal dyneins in human airway epithelia.Journal of cell science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
22 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.