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@CireniaSketches / CNIO.
Chaperone proteins function as highly skilled workers that help other proteins to fold correctly, thus preventing diseases resulting from misfolding.
The CaixaResearch Frontiers Meeting 'Molecular chaperones in cancer and protein quality control' brings together twenty specialists who will present the latest advances in the relationship between chaperones and cancer.
We function thanks to the functioning of our proteins, the biological nanostructures that make us up and of which our organism has tens of thousands of types. Chaperone proteins are a key component in the machinery that makes proteins. They are proteins that, as highly skilled workers, help other proteins to fold correctly. Protein folding is basic; proteins work by fitting together with other molecules like the pieces of a tetris game, and their three-dimensional shape –which determines which molecules they fit together with– depends on how they are folded.
Failures in protein folding and in the correct assembly of multi-protein complexes, especially magnified under cellular stress, lead to diseases, including cancer, and compounds that target chaperones or that correct protein folding are being studied because their potential for the treatment of various diseases, including cancer.
Links between chaperones and cancer
At the CaixaResearch Frontiers Meeting Molecular chaperones in cancer and protein quality control, which starts today at the Spanish National Cancer Research Center (CNIO) with support from ‘la Caixa’ Foundation, about twenty experts in chaperone research and cellular control of protein quality will present the latest advances in the relationship between these proteins and cancer.
“Molecular chaperones play a crucial role in the maintenance of protein folding, stability and function in both normal and pathological states, including cancer,” the organizers explain. “Despite significant advances in recent years, our understanding of the role of chaperones in the development of cancer and other diseases remains incomplete. This conference will focus on recent advances in elucidating the structure and function of chaperones. In addition, we will explore the role of chaperones and of cellular control of protein folding and quality in human diseases, including cancer, as well as new approaches to using chaperones and chaperone-regulated pathways in the treatment of cancer and other diseases.”
ORGANIZERS: Gabriela Chiosis, Memorial Sloan Kettering Institute, NY, US – Nabil Djouder, CNIO, Madrid, Spain – Judith Frydman, Stanford University, US – Oscar Llorca, CNIO, Madrid, Spain – Paul Workman,The Institute of Cancer Research, London, UK.