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  1. Article ; Online: Author Correction: The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium.

    Maurizy, Chloé / Abeza, Claire / Lemmers, Bénédicte / Gabola, Monica / Longobardi, Ciro / Pinet, Valérie / Ferrand, Marina / Paul, Conception / Bremond, Julie / Langa, Francina / Gerbe, François / Jay, Philippe / Verheggen, Céline / Tinari, Nicola / Helmlinger, Dominique / Lattanzio, Rossano / Bertrand, Edouard / Hahne, Michael / Pradet-Balade, Bérengère

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 6200

    Language English
    Publishing date 2022-10-19
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-33519-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Inhibition of Proteasome Activity Induces Formation of Alternative Proteasome Complexes.

    Welk, Vanessa / Coux, Olivier / Kleene, Vera / Abeza, Claire / Trümbach, Dietrich / Eickelberg, Oliver / Meiners, Silke

    The Journal of biological chemistry

    2016  Volume 291, Issue 25, Page(s) 13147–13159

    Abstract: The proteasome is an intracellular protease complex consisting of the 20S catalytic core and its associated regulators, including the 19S complex, PA28αβ, PA28γ, PA200, and PI31. Inhibition of the proteasome induces autoregulatory de novo formation of ... ...

    Abstract The proteasome is an intracellular protease complex consisting of the 20S catalytic core and its associated regulators, including the 19S complex, PA28αβ, PA28γ, PA200, and PI31. Inhibition of the proteasome induces autoregulatory de novo formation of 20S and 26S proteasome complexes. Formation of alternative proteasome complexes, however, has not been investigated so far. We here show that catalytic proteasome inhibition results in fast recruitment of PA28γ and PA200 to 20S and 26S proteasomes within 2-6 h. Rapid formation of alternative proteasome complexes did not involve transcriptional activation of PA28γ and PA200 but rather recruitment of preexisting activators to 20S and 26S proteasome complexes. Recruitment of proteasomal activators depended on the extent of active site inhibition of the proteasome with inhibition of β5 active sites being sufficient for inducing recruitment. Moreover, specific inhibition of 26S proteasome activity via siRNA-mediated knockdown of the 19S subunit RPN6 induced recruitment of only PA200 to 20S proteasomes, whereas PA28γ was not mobilized. Here, formation of alternative PA200 complexes involved transcriptional activation of the activator. Alternative proteasome complexes persisted when cells had regained proteasome activity after pulse exposure to proteasome inhibitors. Knockdown of PA28γ sensitized cells to proteasome inhibitor-mediated growth arrest. Thus, formation of alternative proteasome complexes appears to be a formerly unrecognized but integral part of the cellular response to impaired proteasome function and altered proteostasis.
    MeSH term(s) Autoantigens/metabolism ; Bortezomib/pharmacology ; Cells, Cultured ; Gene Knockdown Techniques ; Humans ; Nuclear Proteins/metabolism ; Oligopeptides/pharmacology ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors/pharmacology ; Protein Multimerization ; Transcription, Genetic
    Chemical Substances Autoantigens ; Ki antigen ; Nuclear Proteins ; ONX 0912 ; Oligopeptides ; Proteasome Inhibitors ; proteasome activator 200 kDa, human ; Bortezomib (69G8BD63PP) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2016-04-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.717652
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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  3. Article ; Online: The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium.

    Maurizy, Chloé / Abeza, Claire / Lemmers, Bénédicte / Gabola, Monica / Longobardi, Ciro / Pinet, Valérie / Ferrand, Marina / Paul, Conception / Bremond, Julie / Langa, Francina / Gerbe, François / Jay, Philippe / Verheggen, Céline / Tinari, Nicola / Helmlinger, Dominique / Lattanzio, Rossano / Bertrand, Edouard / Hahne, Michael / Pradet-Balade, Bérengère

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 4810

    Abstract: The R2TP chaperone cooperates with HSP90 to integrate newly synthesized proteins into multi-subunit complexes, yet its role in tissue homeostasis is unknown. Here, we generated conditional, inducible knock-out mice for Rpap3 to inactivate this core ... ...

    Abstract The R2TP chaperone cooperates with HSP90 to integrate newly synthesized proteins into multi-subunit complexes, yet its role in tissue homeostasis is unknown. Here, we generated conditional, inducible knock-out mice for Rpap3 to inactivate this core component of R2TP in the intestinal epithelium. In adult mice, Rpap3 invalidation caused destruction of the small intestinal epithelium and death within 10 days. Levels of R2TP substrates decreased, with strong effects on mTOR, ATM and ATR. Proliferative stem cells and progenitors deficient for Rpap3 failed to import RNA polymerase II into the nucleus and they induced p53, cell cycle arrest and apoptosis. Post-mitotic, differentiated cells did not display these alterations, suggesting that R2TP clients are preferentially built in actively proliferating cells. In addition, high RPAP3 levels in colorectal tumors from patients correlate with bad prognosis. Here, we show that, in the intestine, the R2TP chaperone plays essential roles in normal and tumoral proliferation.
    MeSH term(s) Animals ; Cell Proliferation ; Cells, Cultured ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Intestinal Mucosa/cytology ; Intestinal Mucosa/metabolism ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; Microscopy, Confocal ; Molecular Chaperones/metabolism ; Protein Binding ; Stem Cells/cytology ; Stem Cells/metabolism ; Mice
    Chemical Substances HSP90 Heat-Shock Proteins ; Molecular Chaperones
    Language English
    Publishing date 2021-08-10
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-021-24792-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones.

    Malinová, Anna / Cvačková, Zuzana / Matějů, Daniel / Hořejší, Zuzana / Abéza, Claire / Vandermoere, Franck / Bertrand, Edouard / Staněk, David / Verheggen, Céline

    The Journal of cell biology

    2017  Volume 216, Issue 6, Page(s) 1579–1596

    Abstract: Splicing is catalyzed by the spliceosome, a complex of five major small nuclear ribonucleoprotein particles (snRNPs). The pre-mRNA splicing factor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central ... ...

    Abstract Splicing is catalyzed by the spliceosome, a complex of five major small nuclear ribonucleoprotein particles (snRNPs). The pre-mRNA splicing factor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central module of the spliceosome. Using quantitative proteomics, we identified assembly intermediates containing PRPF8, EFTUD2, and SNRNP200 in association with the HSP90/R2TP complex, its ZNHIT2 cofactor, and additional proteins. HSP90 and R2TP bind unassembled U5 proteins in the cytoplasm, stabilize them, and promote the formation of the U5 snRNP. We further found that PRPF8 mutants causing Retinitis pigmentosa assemble less efficiently with the U5 snRNP and bind more strongly to R2TP, with one mutant retained in the cytoplasm in an R2TP-dependent manner. We propose that the HSP90/R2TP chaperone system promotes the assembly of a key module of U5 snRNP while assuring the quality control of PRPF8. The proteomics data further reveal new interactions between R2TP and the tuberous sclerosis complex (TSC), pointing to a potential link between growth signals and the assembly of key cellular machines.
    MeSH term(s) Calcium-Binding Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; HeLa Cells ; Humans ; Multiprotein Complexes ; Mutation ; Peptide Elongation Factors/genetics ; Peptide Elongation Factors/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Stability ; Proteomics/methods ; RNA Interference ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Retinitis Pigmentosa/genetics ; Retinitis Pigmentosa/metabolism ; Ribonucleoprotein, U1 Small Nuclear/metabolism ; Ribonucleoprotein, U4-U6 Small Nuclear/metabolism ; Ribonucleoprotein, U5 Small Nuclear/genetics ; Ribonucleoprotein, U5 Small Nuclear/metabolism ; Transfection
    Chemical Substances Calcium-Binding Proteins ; EFTUD2 protein, human ; HSP90 Heat-Shock Proteins ; Multiprotein Complexes ; PRPF8 protein, human ; Peptide Elongation Factors ; RNA Precursors ; RNA, Messenger ; RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear ; Ribonucleoprotein, U4-U6 Small Nuclear ; Ribonucleoprotein, U5 Small Nuclear ; TSC protein, human
    Language English
    Publishing date 2017-06-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201701165
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.190: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.

    Maurizy, Chloé / Quinternet, Marc / Abel, Yoann / Verheggen, Céline / Santo, Paulo E / Bourguet, Maxime / C F Paiva, Ana / Bragantini, Benoît / Chagot, Marie-Eve / Robert, Marie-Cécile / Abeza, Claire / Fabre, Philippe / Fort, Philippe / Vandermoere, Franck / M F Sousa, Pedro / Rain, Jean-Christophe / Charpentier, Bruno / Cianférani, Sarah / Bandeiras, Tiago M /
    Pradet-Balade, Bérengère / Manival, Xavier / Bertrand, Edouard

    Nature communications

    2018  Volume 9, Issue 1, Page(s) 2093

    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 ... ...

    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.
    MeSH term(s) ATPases Associated with Diverse Cellular Activities/metabolism ; Adaptor Proteins, Signal Transducing/metabolism ; Antigens, Surface/metabolism ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; DNA Helicases/metabolism ; GTP-Binding Proteins/metabolism ; HEK293 Cells ; HSP90 Heat-Shock Proteins/metabolism ; HeLa Cells ; Humans ; Male ; Membrane Proteins/metabolism ; Molecular Chaperones/metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Signal Transduction ; Testis/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Antigens, Surface ; Apoptosis Regulatory Proteins ; Carrier Proteins ; HSP90 Heat-Shock Proteins ; Membrane Proteins ; Molecular Chaperones ; PIH1D1 protein, human ; PPFIA2 protein, human ; RPAP3 protein, human ; GTP-Binding Proteins (EC 3.6.1.-) ; SPAG1 protein, human (EC 3.6.1.-) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; DNA Helicases (EC 3.6.4.-) ; RUVBL1 protein, human (EC 3.6.4.12) ; RUVBL2 protein, human (EC 3.6.4.12)
    Language English
    Publishing date 2018-05-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-018-04431-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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