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This Article Full Text Full Text (PDF) All Versions of this Article: JME-08-0116v1 42/1/1    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Web of Science (1) Citing Articles via Google Scholar Google Scholar Articles by Meimaridou, E. Articles by Chapple, J P. Search for Related Content PubMed PubMed Citation Articles by Meimaridou, E. Articles by Chapple, J P.

Centre for Endocrinology, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, London EC1M 6BQ, UK

(Correspondence should be addressed to J P Chapple; Email: j.p.chapple{at}qmul.ac.uk)

Molecular 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.