Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone

The Hsp70/Hsp40 system plays an important role in maintaining cellular proteostasis but so far it is not well understood how Hsp70 proteins are recruited to specific Hsp40 co-chaperones. Here, the authors combine biochemical and biophysical approaches to characterise the oligomeric mammalian Hsp40 D...

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Autores principales: Bryan D. Ryder, Irina Matlahov, Sofia Bali, Jaime Vaquer-Alicea, Patrick C. A. van der Wel, Lukasz A. Joachimiak
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/60d78f39be754f40b8a931a46a1f1dfb
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spelling oai:doaj.org-article:60d78f39be754f40b8a931a46a1f1dfb2021-12-02T14:10:56ZRegulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone10.1038/s41467-021-21147-x2041-1723https://doaj.org/article/60d78f39be754f40b8a931a46a1f1dfb2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21147-xhttps://doaj.org/toc/2041-1723The Hsp70/Hsp40 system plays an important role in maintaining cellular proteostasis but so far it is not well understood how Hsp70 proteins are recruited to specific Hsp40 co-chaperones. Here, the authors combine biochemical and biophysical approaches to characterise the oligomeric mammalian Hsp40 DnaJB8. They identify an intra-oligomer DnaJB8 interaction between the N-terminal J-Domain and the C-terminal domain that occludes the J-Domain surface that binds Hsp70 and propose a model for DnaJB8-Hsp70 recruitment.Bryan D. RyderIrina MatlahovSofia BaliJaime Vaquer-AliceaPatrick C. A. van der WelLukasz A. JoachimiakNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Bryan D. Ryder
Irina Matlahov
Sofia Bali
Jaime Vaquer-Alicea
Patrick C. A. van der Wel
Lukasz A. Joachimiak
Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
description The Hsp70/Hsp40 system plays an important role in maintaining cellular proteostasis but so far it is not well understood how Hsp70 proteins are recruited to specific Hsp40 co-chaperones. Here, the authors combine biochemical and biophysical approaches to characterise the oligomeric mammalian Hsp40 DnaJB8. They identify an intra-oligomer DnaJB8 interaction between the N-terminal J-Domain and the C-terminal domain that occludes the J-Domain surface that binds Hsp70 and propose a model for DnaJB8-Hsp70 recruitment.
format article
author Bryan D. Ryder
Irina Matlahov
Sofia Bali
Jaime Vaquer-Alicea
Patrick C. A. van der Wel
Lukasz A. Joachimiak
author_facet Bryan D. Ryder
Irina Matlahov
Sofia Bali
Jaime Vaquer-Alicea
Patrick C. A. van der Wel
Lukasz A. Joachimiak
author_sort Bryan D. Ryder
title Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
title_short Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
title_full Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
title_fullStr Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
title_full_unstemmed Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
title_sort regulatory inter-domain interactions influence hsp70 recruitment to the dnajb8 chaperone
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/60d78f39be754f40b8a931a46a1f1dfb
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AT jaimevaqueralicea regulatoryinterdomaininteractionsinfluencehsp70recruitmenttothednajb8chaperone
AT patrickcavanderwel regulatoryinterdomaininteractionsinfluencehsp70recruitmenttothednajb8chaperone
AT lukaszajoachimiak regulatoryinterdomaininteractionsinfluencehsp70recruitmenttothednajb8chaperone
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