TAILIEUCHUNG - Báo cáo khoa học: Protein folding and disulfide bond formation in the eukaryotic cell

The endoplasmic reticulum (ER) plays a critical role as a compartment for protein folding in eukaryotic cells. Defects in protein folding contribute to a growing list of diseases, and advances in our understanding of the molec-ular details of protein folding are helping to provide more efficient ways of producing recombinant proteins for industrial and medicinal use. | ỊFEBS Journal MEETING REPORT Protein folding and disulfide bond formation in the eukaryotic cell Meeting report based on the presentations at the European Network Meeting on Protein Folding and Disulfide Bond Formation 2009 Elsinore Denmark Adam M. Benham Biologicaland BiomedicalSciences Durham University UK Keywords chaperone endoplasmic reticulum mitochondria protein disulfide isomerase protein folding redox regulation Correspondence A. Benham Biologicaland Biomedical Sciences Durham University South Road Durham DH1 3LE UK Fax 44 191 334 1201 Tel 44 191 334 1259 E-mail Received 19 August 2009 revised 23 September 2009 accepted 25 September 2009 doi The endoplasmic reticulum ER plays a critical role as a compartment for protein folding in eukaryotic cells. Defects in protein folding contribute to a growing list of diseases and advances in our understanding of the molecular details of protein folding are helping to provide more efficient ways of producing recombinant proteins for industrial and medicinal use. Moreover research performed in recent years has shown the importance of the ER as a signalling compartment that contributes to overall cellular homeostasis. Hamlet s castle provided a stunning backdrop for the latest European network meeting to discuss this subject matter in Elsinore Denmark from 3 to 5 June 2009. Organized by researchers at the Department of Biology University of Copenhagen the meeting featured 20 talks by both established names and younger scientists focusing on topics such as oxidative protein folding and maturation in particular in the ER but also in other compartments cellular redox regulation ER-associated degradation and the unfolded protein response. Exciting new advances were presented and the intimate setting with about 50 participants provided an excellent opportunity to discuss current key questions in the field. Introduction Protein folding in a living cell does not usually

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