HSP90 and the R2TP co-chaperone complex: Building multi-protein machineries essential for cell growth and gene expression
HSP90 (Heat Shock Protein 90) is an essential chaperone involved in the last folding steps of client proteins. It has many clients, and these are often recognized through specific adaptors. Recently, the conserved R2TP complex was identified as a key HSP90 co-chaperone. Current evidences indicate th...
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| Veröffentlicht in: | RNA biology 2012-02, Vol.9 (2), p.148-154 |
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| creator | Boulon, Séverine Bertrand, Edouard Pradet-Balade, Bérengère |
| description | HSP90 (Heat Shock Protein 90) is an essential chaperone involved in the last folding steps of client proteins. It has many clients, and these are often recognized through specific adaptors. Recently, the conserved R2TP complex was identified as a key HSP90 co-chaperone. Current evidences indicate that the HSP90/R2TP system assembles multi-molecular protein complexes. Strikingly, these comprise basic machineries of gene expression: (1) nuclear RNA polymerases; (2) the snoRNPs, essential to produce ribosomes; and (3) mTOR Complex 1 and 2, which control translational activity and cell growth. Another important substrate is the telomerase RNP, required for continuous cell proliferation. We discuss here the assembly of RNA polymerases in bacteria and eukaryotes, the role of HSP90/R2TP in this process and in the assembly of snoRNPs and the PIKK family of TORC1 kinase. Finally, we speculate on the roles of R2TP as a master regulator of cell growth under normal or pathological conditions. |
| doi_str_mv | 10.4161/rna.18494 |
| format | Article |
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Finally, we speculate on the roles of R2TP as a master regulator of cell growth under normal or pathological conditions.</description><identifier>ISSN: 1547-6286</identifier><identifier>EISSN: 1555-8584</identifier><identifier>DOI: 10.4161/rna.18494</identifier><identifier>PMID: 22418846</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Binding ; Biochemistry, Molecular Biology ; Biology ; Bioscience ; Calcium ; Cancer ; Cell ; Cell Proliferation ; complex assembly ; Cycle ; Gene Expression Regulation ; HSP90 ; HSP90 Heat-Shock Proteins - metabolism ; Landes ; Life Sciences ; Models, Biological ; Molecular Chaperones - metabolism ; Multiprotein Complexes - metabolism ; NMD ; Nuclear Proteins - metabolism ; Organogenesis ; PIKK ; Protein Binding ; protein synthesis ; Proteins ; R2TP ; Ribonucleoproteins, Small Nucleolar - metabolism ; RNA polymerase ; RNA Polymerase II - metabolism ; snoRNP</subject><ispartof>RNA biology, 2012-02, Vol.9 (2), p.148-154</ispartof><rights>Copyright © 2012 Landes Bioscience 2012</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4044-e453c8af9cb80474788d182bc7e21cdb865c78cc6a5fac0b347c9255baf297d23</citedby><cites>FETCH-LOGICAL-c4044-e453c8af9cb80474788d182bc7e21cdb865c78cc6a5fac0b347c9255baf297d23</cites><orcidid>0000-0002-9642-7994 ; 0000-0002-5350-7169</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22418846$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00714777$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Boulon, Séverine</creatorcontrib><creatorcontrib>Bertrand, Edouard</creatorcontrib><creatorcontrib>Pradet-Balade, Bérengère</creatorcontrib><title>HSP90 and the R2TP co-chaperone complex: Building multi-protein machineries essential for cell growth and gene expression</title><title>RNA biology</title><addtitle>RNA Biol</addtitle><description>HSP90 (Heat Shock Protein 90) is an essential chaperone involved in the last folding steps of client proteins. It has many clients, and these are often recognized through specific adaptors. Recently, the conserved R2TP complex was identified as a key HSP90 co-chaperone. Current evidences indicate that the HSP90/R2TP system assembles multi-molecular protein complexes. Strikingly, these comprise basic machineries of gene expression: (1) nuclear RNA polymerases; (2) the snoRNPs, essential to produce ribosomes; and (3) mTOR Complex 1 and 2, which control translational activity and cell growth. Another important substrate is the telomerase RNP, required for continuous cell proliferation. We discuss here the assembly of RNA polymerases in bacteria and eukaryotes, the role of HSP90/R2TP in this process and in the assembly of snoRNPs and the PIKK family of TORC1 kinase. 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| subjects | Binding Biochemistry, Molecular Biology Biology Bioscience Calcium Cancer Cell Cell Proliferation complex assembly Cycle Gene Expression Regulation HSP90 HSP90 Heat-Shock Proteins - metabolism Landes Life Sciences Models, Biological Molecular Chaperones - metabolism Multiprotein Complexes - metabolism NMD Nuclear Proteins - metabolism Organogenesis PIKK Protein Binding protein synthesis Proteins R2TP Ribonucleoproteins, Small Nucleolar - metabolism RNA polymerase RNA Polymerase II - metabolism snoRNP |
| title | HSP90 and the R2TP co-chaperone complex: Building multi-protein machineries essential for cell growth and gene expression |
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