Molecular chaperonin HSP60 is a highly conserved protein involved in maintaining protein homeostasis, mitochondrial integrity, and cellular stress responses. It exists in two main forms: Group I chaperonins, found in eubacteria and organelles like mitochondria, and Group II chaperonins, present in eukaryotic cytosol. HSP60 is a double-ring structure that facilitates the folding of proteins, protects against oxidative stress, and regulates apoptosis. In mitochondria, it plays a critical role in maintaining mitochondrial function and preventing cell death. HSP60 is also involved in various diseases, including cancer, neurodegeneration, and inflammatory disorders. Its expression is regulated by multiple factors, including transcriptional and post-translational modifications, and it can act as a therapeutic target in various conditions. HSP60 is overexpressed in many cancers, such as colorectal, breast, and lung cancers, and its levels are associated with disease progression and prognosis. In some cancers, HSP60 promotes tumor growth, while in others, it may have a protective role. HSP60 is also involved in immune responses, with its expression on the cell surface contributing to immune signaling and autoantibody formation. In inflammatory diseases, HSP60 can trigger pro-inflammatory responses and contribute to tissue damage. HSP60 is found in various subcellular locations, including the cytoplasm, mitochondria, and cell surface, and its localization can influence its functional roles. HSP60 is also present in exosomes and can be used as a biomarker for various diseases. Research on HSP60 is ongoing, with a focus on understanding its diverse functions and potential therapeutic applications.Molecular chaperonin HSP60 is a highly conserved protein involved in maintaining protein homeostasis, mitochondrial integrity, and cellular stress responses. It exists in two main forms: Group I chaperonins, found in eubacteria and organelles like mitochondria, and Group II chaperonins, present in eukaryotic cytosol. HSP60 is a double-ring structure that facilitates the folding of proteins, protects against oxidative stress, and regulates apoptosis. In mitochondria, it plays a critical role in maintaining mitochondrial function and preventing cell death. HSP60 is also involved in various diseases, including cancer, neurodegeneration, and inflammatory disorders. Its expression is regulated by multiple factors, including transcriptional and post-translational modifications, and it can act as a therapeutic target in various conditions. HSP60 is overexpressed in many cancers, such as colorectal, breast, and lung cancers, and its levels are associated with disease progression and prognosis. In some cancers, HSP60 promotes tumor growth, while in others, it may have a protective role. HSP60 is also involved in immune responses, with its expression on the cell surface contributing to immune signaling and autoantibody formation. In inflammatory diseases, HSP60 can trigger pro-inflammatory responses and contribute to tissue damage. HSP60 is found in various subcellular locations, including the cytoplasm, mitochondria, and cell surface, and its localization can influence its functional roles. HSP60 is also present in exosomes and can be used as a biomarker for various diseases. Research on HSP60 is ongoing, with a focus on understanding its diverse functions and potential therapeutic applications.