The present invention relates to a mutated heat-shock protein 110 (HSP110) lacking its substrate binding domain, which does not exhibit its chaperone activity and/or is not capable of binding to heat-shock protein 70 (HSP70) and/or to heat-shock protein 27 (HSP27), but which is capable of binding to a wild-type HSP110. Such a mutated heat-shock protein 110 can be used (i) in methods for prognosing survival and/or the response to a treatment of a patient suffering from a cancer, more particularly from a cancer liable to have a microsatellite instability (MSI) phenotype, such as colorectal cancer (CRC), and (ii) for treating cancers.