RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.

Larissa M Antonio, Carlos H I Ramos

Abstract readReview

In one paragraph

Review in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Larissa M AntonioInstitute of Chemistry, University of Campinas (UNICAMP), Campinas, São Paulo, Brazil; National Institute of Science and Technology for Bioimage and Structural Biology INBEB, Rio de Janeiro, Rio de Janeiro, Brazil.

Carlos H I RamosInstitute of Chemistry, University of Campinas (UNICAMP), Campinas, São Paulo, Brazil; National Institute of Science and Technology for Bioimage and Structural Biology INBEB, Rio de Janeiro, Rio de Janeiro, Brazil. Electronic address: cramos@unicamp.br.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functional versatility of Hsp90 relies on its association with specialized co-chaperones that regulate client recruitment and maturation. Among these, the R2TP complex, comprising RUVBL1, RUVBL2, RPAP3 (Tah1 in yeast), and PIH1D1, acts as a conserved assembly factor essential for the biogenesis of large multiprotein machineries, including RNA polymerases, snoRNPs, PIKKs, and mTOR signaling complexes. RPAP3 functions as a central scaffold within the R2TP-Hsp90 system, linking Hsp90 and Hsp70 to the RUVBL1/2 ATPase core through its TPR domains and C-terminal interaction with PIH1D1. This modular organization enables RPAP3 to integrate chaperone-mediated folding with client delivery and complex assembly. Notably, dysregulation of RPAP3 has been implicated in oncogenic processes, highlighting its biomedical relevance. This review synthesizes current structural, functional, and evolutionary insights into RPAP3, focusing on its role within the R2TP-Hsp90 machinery and its emerging connections to human disease.

Indexed as

Evolution, MolecularMolecular ChaperonesApoptosis Regulatory ProteinsHSP90 Heat-Shock ProteinsHumansApoptosis Regulatory ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesRPAP3 protein, humanHsp90PIH1D1protein homeostasisR2TPRPAP3

Identifiers

PMID41966271

DOI10.1016/j.jbc.2026.111439

PMCPMC13153604

What Socratic holds

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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 Socratic graph.