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                  <mods:namePart>Rodríguez, Carlos F</mods:namePart>
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                  <mods:namePart>Llorca, Oscar</mods:namePart>
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                  <mods:namePart>Llorca Blanco, Oscar Antonio</mods:namePart>
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                  <mods:dateAccessioned encoding="iso8601">2024-09-16T08:16:57Z</mods:dateAccessioned>
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               <mods:identifier type="citation">Cells  . 2020 ;9(5):1139</mods:identifier>
               <mods:identifier type="uri">https://hdl.handle.net/20.500.12105/23085</mods:identifier>
               <mods:identifier type="pubmedID">32384603</mods:identifier>
               <mods:identifier type="doi">10.3390/cells9051139</mods:identifier>
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               <mods:identifier type="journal">Cells</mods:identifier>
               <mods:abstract>The Rvb1-Rvb2-Tah1-Pih1 (R2TP) complex is a co-chaperone complex that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II (Pol II) and complexes of the phosphatidylinositol-3-kinase-like family of kinases (PIKKs), such as mTORC1 and ATR/ATRIP. R2TP is made of four subunits: RuvB-like protein 1 (RUVBL1) and RuvB-like 2 (RUVBL2) AAA-type ATPases, RNA polymerase II-associated protein 3 (RPAP3), and the Protein interacting with Hsp90 1 (PIH1) domain-containing protein 1 (PIH1D1). R2TP associates with other proteins as part of a complex co-chaperone machinery involved in the assembly and maturation of a growing list of macromolecular complexes. Recent progress in the structural characterization of R2TP has revealed an alpha-helical domain at the C-terminus of RPAP3 that is essential to bring the RUVBL1 and RUVBL2 ATPases to R2TP. The RPAP3 C-terminal domain interacts directly with RUVBL2 and it is also known as RUVBL2-binding domain (RBD). Several human proteins contain a region homologous to the RPAP3 C-terminal domain, and some are capable of assembling R2TP-like complexes, which could have specialized functions. Only the RUVBL1-RUVBL2 ATPase complex and a protein containing an RPAP3 C-terminal-like domain are found in all R2TP and R2TP-like complexes. Therefore, the RPAP3 C-terminal domain is one of few components essential for the formation of all R2TP and R2TP-like co-chaperone complexes.</mods:abstract>
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                  <mods:title>RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes.</mods:title>
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