RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes
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 a...
Main Authors: | , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2020-05-01
|
Series: | Cells |
Subjects: | |
Online Access: | https://www.mdpi.com/2073-4409/9/5/1139 |
id |
doaj-d2d31070d60f4685a3fd96f7236d2d00 |
---|---|
record_format |
Article |
spelling |
doaj-d2d31070d60f4685a3fd96f7236d2d002020-11-25T02:07:12ZengMDPI AGCells2073-44092020-05-0191139113910.3390/cells9051139RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone ComplexesCarlos F. Rodríguez0Oscar Llorca1Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, 28029 Madrid, SpainStructural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, 28029 Madrid, SpainThe 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.https://www.mdpi.com/2073-4409/9/5/1139RUVBL1RUVBL2RPAP3PIH1D1R2TPHSP90 co-chaperone |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Carlos F. Rodríguez Oscar Llorca |
spellingShingle |
Carlos F. Rodríguez Oscar Llorca RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes Cells RUVBL1 RUVBL2 RPAP3 PIH1D1 R2TP HSP90 co-chaperone |
author_facet |
Carlos F. Rodríguez Oscar Llorca |
author_sort |
Carlos F. Rodríguez |
title |
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes |
title_short |
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes |
title_full |
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes |
title_fullStr |
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes |
title_full_unstemmed |
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes |
title_sort |
rpap3 c-terminal domain: a conserved domain for the assembly of r2tp co-chaperone complexes |
publisher |
MDPI AG |
series |
Cells |
issn |
2073-4409 |
publishDate |
2020-05-01 |
description |
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. |
topic |
RUVBL1 RUVBL2 RPAP3 PIH1D1 R2TP HSP90 co-chaperone |
url |
https://www.mdpi.com/2073-4409/9/5/1139 |
work_keys_str_mv |
AT carlosfrodriguez rpap3cterminaldomainaconserveddomainfortheassemblyofr2tpcochaperonecomplexes AT oscarllorca rpap3cterminaldomainaconserveddomainfortheassemblyofr2tpcochaperonecomplexes |
_version_ |
1724930814250057728 |