It was later shown in ovarian cancer cells that HSP90-MLK3 dissociation induced by geldanamycin facilitated association of MLK3 with HSP70 and its co-chaperone E3 ligase carboxyl terminus of Hsc70-interacting protein (CHIP), followed by E2 ubiquitin-conjugating enzyme UbcH5a, -b, -c and -d, resulting in MLK3 ubiquitination and degradation via proteasome pathway [63] (Figure 3). The gene discussed is MAP3K11; the disease is ovarian carcinoma.