Abstract
Heat-shock proteins have been found to form part of a large protein complex, called the epichaperome, that improves the survival of some cancer cells. This complex might offer a new target for cancer treatment. See Letter p.397 The chaperome describes the assembly of chaperones, co-chaperones, adaptors and folding enzymes into dynamic complexes that regulate cellular homeostasis. Whereas in normal cells, these assemblies are transient, Gabriela Chiosis and colleagues show that under conditions of stress, such as cancer, the chaperome forms a stable network that aids deleterious cell survival. The authors investigate the presence of such larger 'epichaperome' complexes in patient samples and find that they occur irrespective of tissue of origin or genetic background, and can be present in more than half of all cancers. These findings hint that targeting the epichaperome, rather than the chaperome components, could lead the way for developing new cancer treatments.
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