Impacts of Heat Shock Protein 40/J-domain Proteins on Cancer Progression and p53 Activity

The p53 tumor suppressor is frequently mutated in various types of cancer. Majority mutations are missense mutations, which results not only loss the suppressive activity (loss function), but also acquirement unexpected oncogenic activities, referred to as gain function (GOF). Although stability and accumulation wild-type (wtp53) mutant (mutp53) proteins crucial exhibit respectively, underlying mechanisms remain unclear. Heat shock (HSPs) one major molecular chaperones have a variety functions including protein folding, transportation, stabilization degradation misfolded or denatured proteins. Of HSP family, HSP40, known J-domain (JDPs), largest family with over fifty members contains highly conserved J domain. HSP40/JDPs mainly co-chaperone HSP70 stimulate ATPase through interactions between domain HSP70. Increasing evidence indicates regulate levels activities wtp53 mutp53. Here, we introduce our recent studies regarding roles DNAJA1 conformational mutp53 cancer metastasis, summarize updated information related regulation by HSP40/JDPs.