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)
    
    
    
		
		
			
				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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        Publikationstyp
        Artikel: Journalartikel
    
 
    
        Dokumenttyp
        Wissenschaftlicher Artikel
    
 
    
        Typ der Hochschulschrift
        
    
 
    
        Herausgeber
        
    
    
        Schlagwörter
        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
    
 
    
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        Sprache
        englisch
    
 
    
        Veröffentlichungsjahr
        2022
    
 
    
        Prepublished im Jahr 
        
    
 
    
        HGF-Berichtsjahr
        2022
    
 
    
    
        ISSN (print) / ISBN
        1097-2765
    
 
    
        e-ISSN
        1097-4164
    
 
    
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	    Band: 82,  
	    Heft: 3,  
	    Seiten: 555-569.e7 
	    Artikelnummer: ,  
	    Supplement: ,  
	
    
 
  
        
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            Verlag
            Elsevier
        
 
        
            Verlagsort
            50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
        
 
	
        
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        Begutachtungsstatus
        Peer reviewed
    
 
     
    
        POF Topic(s)
        30203 - Molecular Targets and Therapies
    
 
    
        Forschungsfeld(er)
        Enabling and Novel Technologies
    
 
    
        PSP-Element(e)
        G-503000-001
    
 
    
        Förderungen
        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
    
 
    
        Copyright
        
    
 	
    
    
    
    
    
        Erfassungsdatum
        2022-02-08