Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
 
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve
Pubget Overpricing |  
lüll
From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery Meimaridou E; Gooljar SB; Chapple JPJ Mol Endocrinol 2009[Jan]; 42 (1): 1-9Molecular chaperones are best recognized for their roles in de novo protein folding and the cellular response to stress. However, many molecular chaperones, and in particular the Hsp70 chaperone machinery, have multiple diverse cellular functions. At the molecular level, chaperones are mediators of protein conformational change. To facilitate conformational change of client/substrate proteins, in manifold contexts, chaperone power must be closely regulated and harnessed to specific cellular locales--this is controlled by cochaperones. This review considers specialized functions of the Hsp70 chaperone machinery mediated by its cochaperones. We focus on vesicular trafficking, protein degradation and a potential role in G protein-coupled receptor processing.|Animals[MESH]|Endocytosis/physiology[MESH]|Exocytosis/physiology[MESH]|HSP70 Heat-Shock Proteins/*metabolism[MESH]|Humans[MESH]|Models, Molecular[MESH]|Molecular Chaperones/*metabolism[MESH]|Proteasome Endopeptidase Complex/metabolism[MESH]|Protein Conformation[MESH]|Protein Folding[MESH]|Receptors, G-Protein-Coupled/metabolism[MESH] |
