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The cell biology of the chaperonins (Cpns) has been intensively studied over the past 25 years. These ubiquitous and essential molecules assist proteins to fold into their native state and function to protect proteins from denaturation after stress. The structure of the most widely studied Cpn60, Escherichia coli GroEL, has been solved and its mechanism of protein folding action largely established. But in the last decade, evidence has accumulated to suggest that the Cpn60s have functions in addition to intracellular protein folding, particularly the ability to act as intercellular signals with a wide variety of biological effects. Cpn60 has the ability to stimulate cells to produce proinflammatory cytokines and other proteins involved in immunity and inflammation and may, therefore, provide a link between innate and adaptive immunity. Cpn60s are also thought to be pathogenic factors in a wide range of diseases and have recently been reported to be present in the circulation of normal subjects and those with heart disease. An interesting facet of these proteins is the finding that in spite of significant sequence conservation, individual Cpn60 proteins can express very different biological activities. This review discusses the work to date, which has revealed the cell-cell signaling actions of Cpn60 proteins.

Chaperonin 60 unfolds its secrets of cellular communication