The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium

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

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)

RPAP3 is a subunit of the R2TP complex, a co-chaperone of HSP90, with substrate proteins involved in transcription, ribosome biogenesis, DNA repair and cell growth. Here the authors report that deletion of Rpap3 abrogates cell proliferation and homeo

Externí odkaz: https://doaj.org/article/a94c9c9c3f30427b974454354a00e279

The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones

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

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)

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

Externí odkaz: https://doaj.org/article/f9bce095aa2a4c49a49a7a66e4c6ecf6

Deciphering cellular and molecular determinants of human DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases

Autor: Raphael Dos Santos Morais, Paulo E. Santo, Marie Ley, Cédric Schelcher, Yoann Abel, Laura Plassart, Evolène Deslignière, Marie-Eve Chagot, Marc Quinternet, Ana C.F. Paiva, Steve Hessmann, Nelly Morellet, Pedro M. F. Sousa, Franck Vandermoere, Edouard Bertrand, Bruno Charpentier, Tiago M. Bandeiras, Célia Plisson-Chastang, Céline Verheggen, Sarah Cianférani, Xavier Manival

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2022, 434 (19), pp.167760. ⟨10.1016/j.jmb.2022.167760⟩
Journal of Molecular Biology, 2022, 434 (19), pp.167760. ⟨10.1016/j.jmb.2022.167760⟩

International audience; DPCD is a protein that may play a role in cilia formation and whose absence leads to primary ciliary dyskinesia (PCD), a rare disease caused by impairment of ciliated cells. Except for high-throughput studies that identified D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd345e232f2d8530185141c08a5cbce2
https://hal.archives-ouvertes.fr/hal-03745381

The interaction between RPAP3 and TRBP reveals a possible involvement of the HSP90/R2TP chaperone complex in the regulation of miRNA activity

Autor: Yoann Abel, Christophe Charron, Camille Virciglio, Valérie Bourguignon-Igel, Marc Quinternet, Marie-Eve Chagot, Marie-Cécile Robert, Céline Verheggen, Christiane Branlant, Edouard Bertrand, Xavier Manival, Bruno Charpentier, Mathieu Rederstorff

Publikováno v: Nucleic acids research. 50(4)

MicroRNAs silence mRNAs by guiding the RISC complex. RISC assembly occurs following cleavage of pre-miRNAs by Dicer, assisted by TRBP or PACT, and the transfer of miRNAs to AGO proteins. The R2TP complex is an HSP90 co-chaperone involved in the assem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c98f0cfd2ca86906f8fa821a360a434d
https://pubmed.ncbi.nlm.nih.gov/35150569

The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium

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

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)
Nature Communications
Nature Communications, 2021, 12 (1), pp.4810. ⟨10.1038/s41467-021-24792-4⟩
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.4810. ⟨10.1038/s41467-021-24792-4⟩

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 c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66a684d2b37d0731f7bbb1ca0f5ddd57
https://pubmed.ncbi.nlm.nih.gov/36261420