HSPA12A is an atypical HSP70 family member with context-dependent roles in cellular stress responses and cancer progression. As an adapter protein, HSPA12A modulates protein trafficking and stability through direct protein-protein interactions 1. The protein functions through distinct mechanisms across tissues: in renal cells, HSPA12A destabilizes CD147 via HRD1-mediated ubiquitination to suppress lactate export and migration, acting as a metastasis inhibitor 2. Conversely, in hepatocellular carcinoma, HSPA12A promotes migration by increasing MCT4 membrane localization to enhance lactate export 3. During ischemic stroke and kidney ischemia/reperfusion injury, HSPA12A activates neuroprotective and renoprotective pathways through GSK-3β/mTOR signaling and c-Myc lactylation-mediated proliferation, respectively 41. HSPA12A also promotes M1 macrophage polarization via nuclear PKM2 translocation in nonalcoholic steatohepatitis 5 and impairs cardioprotective lipophagy in sepsis by competing with LC3-II for PNPLA2 binding 6. Genetic variants in HSPA12A associate with reduced gastric cancer risk in Chinese populations 7. Alternative splicing of HSPA12A regulated by SRSF11 influences colorectal cancer metastasis 8. These pleiotropic functions identify HSPA12A as a potential therapeutic target for cancer, cardiovascular, and metabolic diseases.