Abstract
Yeast require the enzyme Hsp104 to untangle protein aggregates, which arise in stressed or aged cells. Animals lack Hsp104, but it emerges that proteins of the DNAJ family of molecular chaperones can fulfil this role. See Letter p.251 Microbes eliminate toxic intracellular protein aggregates thanks to HSP100 disaggregases, which are missing from animal cells. Now Bernd Bukau and colleagues have discovered an efficient protein disaggregation system in metazoan cells, which requires transient interactions between J-protein co-chaperones of classes A and B, which synergistically boost HSP70-dependent disaggregation activity. This system provides a flexible further level of regulation for metazoan protein quality control, with direct relevance to human diseases such as age-related neurodegeneration.
Published Version
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