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The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.

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  • معلومة اضافية
    • بيانات النشر:
      Nature Publishing Group
    • الموضوع:
      2018
    • Collection:
      University of Liège: ORBi (Open Repository and Bibliography)
    • نبذة مختصرة :
      peer reviewed ; 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.
    • ISSN:
      2041-1723
    • Relation:
      urn:issn:2041-1723; https://orbi.uliege.be/handle/2268/259801; info:hdl:2268/259801; https://orbi.uliege.be/bitstream/2268/259801/1/41467_2018_Article_4431.pdf; scopus-id:2-s2.0-85047874307; info:pmid:29844425
    • الرقم المعرف:
      10.1038/s41467-018-04431-1
    • Rights:
      open access ; http://purl.org/coar/access_right/c_abf2 ; info:eu-repo/semantics/openAccess
    • الرقم المعرف:
      edsbas.21B9D658