HSPA9 (Heat Shock Protein Family A (Hsp70) Member 9)

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HSPA9 (Heat Shock Protein Family A (Hsp70) Member 9) also known as mortalin, is a protein that in humans is encoded by the HSPA9 gene. HSPA9 is a highly conserved member of the HSP70 family of proteins. It functions as a chaperone in the mitochondria, cytoplasm, and centrosome. Studies on cancer biology have shown that HSPA9 plays an important role in anti-apoptosis. It works by counteracting the "pressure" of aging and apoptosis and acts as a "microevolutionary buffer" to neutralize the conformational consequences of mutant proteins. It also helps to gain the function of a partner-stable rogue protein and promotes the invasiveness and motility of cells. In addition, HSPA9 plays a key role in overactivation of proliferation signals and cellular coordination of resistance to radiation, heat, hormones and chemotherapy. Diseases associated with HSPA9 include sporadic syndrome and anemia, sideroblasts.

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