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Biebl, M.M.* ; Delhommel, F. ; Faust, O.* ; Zak, K.M. ; Agam, G.* ; Guo, X.* ; Mühlhofer, M.* ; Dahiya, V.* ; Hillebrand, D.* ; Popowicz, G.M. ; Kampmann, M.* ; Lamb, D.C.* ; Rosenzweig, R.* ; Sattler, M. ; Buchner, J.*

NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems.

Mol. Cell 82, 555-569.e7 (2022)
Publ. Version/Full Text Research data DOI PMC
Open Access Hybrid
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In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem with the maturation of a diverse array of client proteins. The transfer of nonnative clients between these systems is essential to the chaperoning process, but how it is regulated is still not clear. We discovered that NudC is an essential transfer factor with an unprecedented mode of action: NudC interacts with Hsp40 in Hsp40-Hsp70-client complexes and displaces Hsp70. Then, the interaction of NudC with Hsp90 allows the direct transfer of Hsp40-bound clients to Hsp90 for further processing. Consistent with this mechanism, NudC increases client activation in vitro as well as in cells and is essential for cellular viability. Together, our results show the complexity of the cooperation between the major chaperone machineries in the eukaryotic cytosol.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Co-chaperones ; Glucocorticoid Receptor ; Hsp40 ; Hsp70 ; Hsp90 ; Molecular Chaperones ; Nmr Spectroscopy ; Nudc ; Protein Folding ; Spfret; Nmr-spectroscopy; Structural-characterization; Hsp90 Atpase; Protein; Hsp70; Binding; P53; Chaperones; Reveals; Crispr
Language english
Publication Year 2022
HGF-reported in Year 2022
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Journal Molecular Cell
Quellenangaben Volume: 82, Issue: 3, Pages: 555-569.e7 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
Grants Bayerisch-Kalifornischen Hochschulzentrum
Abisch-Frenkel-Stiftung
'Deutsche Forschungsgemeinschaft (DFG)'
EC | European Research Council (ERC)
Verband der Chemischen Industrie
European Molecular Biology Organization (EMBO)
Ramona Absmeier and Matina-Jasemi Loukeri
Helmholtz Association Initiative and Networking Funds
DOI 10.1016/j.molcel.2021.12.031
WOS ID WOS:000752546500008
Scopus ID 85123801078
PubMed ID 35063133
Erfassungsdatum 2022-02-08
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