ArticleThe Journal of biological chemistry2014
Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 53 citations in OpenAlex.
- High-throughput mechanomic screening reveals novel regulators of single-cell mechanics.Biophysical journal · 2026Article
- RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.The Journal of biological chemistry · 2026Review
- Co-translational determination of quaternary structures in chaperone factories.Nature communications · 2026Article
- RuvBL1/2 reduce toxic dipeptide repeat protein burden in multiple models of C9orf72-ALS/FTD.Life science alliance · 2025Article
- The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophysical reviews · 2023Review
- Hsp40 overexpression in pacemaker neurons delays circadian dysfunction in a Drosophila model of Huntington's disease.Disease models & mechanisms · 2022Article
- The role of SPAG1 in the assembly of axonemal dyneins in human airway epithelia.Journal of cell science · 2022Article
- Identification and expression analysis of heat-shock proteins in wheat infected with powdery mildew and stripe rust.The plant genome · 2021Article
- The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Archives of toxicology · 2021Review
- Role of the Novel Hsp90 Co-Chaperones in Dynein Arms' Preassembly.International journal of molecular sciences · 2019Review
- Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function.Biophysical reviews · 2019Review
- Prefoldin 6 mediates longevity response from heat shock factor 1 to FOXO inGenes & development · 2018Article
- Differential intracellular localization of Hsp70 in the gill and heart tissue of fresh water prawn Macrobrachium malcolmsonii during thermal stress.Molecular biology reports · 2018Article
- Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP.The Journal of cell biology · 2018Article
- The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.Nature communications · 2018Article
- Article
- Assembly and trafficking of box C/D and H/ACA snoRNPs.RNA biology · 2017Review
- R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein.Nature communications · 2017Article
- Article
- The Proteasome Subunit Rpn8 Interacts with the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-independent Degradation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2016Article
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Authors and funding
14 authors at 8 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2. In mammals, the R2TP is involved in the biogenesis of cellular machineries such as RNA polymerases, small nucleolar ribonucleoparticles and phosphatidylinositol 3-kinase-related kinases. Here, we characterize the spaghetti (spag) gene of Drosophila, the homolog of human RPAP3. This gene plays an essential function during Drosophila development. We show that Spag protein binds Drosophila orthologs of R2TP components and Hsp90, like its yeast counterpart. Unexpectedly, Spag also interacts and stimulates the chaperone activity of Hsp70. Using null mutants and flies with inducible RNAi, we show that spaghetti is necessary for the stabilization of snoRNP core proteins and target of rapamycin activity and likely the assembly of RNA polymerase II. This work highlights the strong conservation of both the HSP90/R2TP system and its clients and further shows that Spag, unlike Saccharomyces cerevisiae Tah1, performs essential functions in metazoans. Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes.
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