Back to Search
Start Over
The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones
- Source :
- Datacite, DOAJ-Articles, Hyper Article en Ligne, PubMed Central, Mémoires en Sciences de l'Information et de la Communication, HAL-Inserm, Repositório da Universidade Nova de Lisboa, Europe PubMed Central, UnpayWall, ORCID, Microsoft Academic Graph, Nature Communications, Nature Publishing Group, 2018, 9 (1), pp.2093. ⟨10.1038/s41467-018-04431-1⟩, Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-018-04431-1⟩, Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018), Nature Communications, Nature Communications, 2018, 9 (1), pp.2093. ⟨10.1038/s41467-018-04431-1⟩, Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP
- Publication Year :
- 2018
- Publisher :
- Springer Science and Business Media LLC, 2018.
-
Abstract
- R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-α2 expression and for the assembly of liprin-α2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 °C, suggesting that R2SP could help compensating the lower temperate of testis.<br />R2TP is an HSP90 co-chaperone composed of an RPAP3-PIH1D1 heterodimer, which binds two essential AAA+ ATPases RUVBL1/RUVBL2. Here authors use a structural approach to study RPAP3 and find an RPAP3-like protein (SPAG1) which also forms a co-chaperone complex with PIH1D2 and RUVBL1/2 enriched in testis.
- Subjects :
- Male
AAA proteins
[SDV]Life Sciences [q-bio]
General Physics and Astronomy
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Chaperone
[SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy
Protein Structure, Secondary
Testis
lcsh:Science
GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries)
ComputingMilieux_MISCELLANEOUS
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
[SDV] Life Sciences [q-bio]
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Antigens, Surface
Protein Binding
Signal Transduction
Cell biology
RUVBL2
Science
[SDV.CAN]Life Sciences [q-bio]/Cancer
Hsp90
Chaperone (protein)
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
Plasma protein binding
Article
General Biochemistry, Genetics and Molecular Biology
Cell Line
GTP-Binding Proteins
Genetics
Humans
GTP-binding protein regulators
HSP90 Heat-Shock Proteins
Protein folding
IP LUMIER
Adaptor Proteins, Signal Transducing
DNA Helicases
Membrane Proteins
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
General Chemistry
liprin-α2
NMR
[SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis
HEK293 Cells
Membrane protein
ATPases Associated with Diverse Cellular Activities
lcsh:Q
Apoptosis Regulatory Proteins
Carrier Proteins
R2SP
HeLa Cells
Molecular Chaperones
Subjects
Details
- ISSN :
- 20411723
- Database :
- OpenAIRE
- Journal :
- Datacite, DOAJ-Articles, Hyper Article en Ligne, PubMed Central, Mémoires en Sciences de l'Information et de la Communication, HAL-Inserm, Repositório da Universidade Nova de Lisboa, Europe PubMed Central, UnpayWall, ORCID, Microsoft Academic Graph, Nature Communications, Nature Publishing Group, 2018, 9 (1), pp.2093. ⟨10.1038/s41467-018-04431-1⟩, Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-018-04431-1⟩, Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018), Nature Communications, Nature Communications, 2018, 9 (1), pp.2093. ⟨10.1038/s41467-018-04431-1⟩, Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP
- Accession number :
- edsair.pmid.dedup....4597d05a6e66cf10473b70c6f7a77a32