The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?

ABSTRACT: Cytosolic heat shock proteins have received significant attention as emerging therapeutic targets. Much of this excitement has been triggered by the discovery that HSP90 plays a central role in the maintenance and stability of multifarious oncogenic membrane receptors and their resultant tyrosine kinase activity. Numerous studies have dealt with the effects of small molecules on chaperone- and stress-related pathways of the endoplasmic reticulum (ER). However, unlike cytosolic chaperones, relatively little emphasis has been placed upon translational avenues towards targeting of the ER for inhibition of folding/secretion of disease-promoting proteins. Here, we summarise existing small molecule inhibitors and potential future targets of ER chaperone-mediated inhibition. Client proteins of tr

SUBMITTER: McLaughlin M 

PROVIDER: S-EPMC3031055 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature