Coupling apoptosis resistance to the cellular stress response: the IAP-Hsp90 connection in cancer.
Understanding how tumor cells manage to survive and proliferate in ever-changing and often harmful microenvironments is a daunting challenge in tumor biology, and a major cause of treatment failure in the oncology clinic. Recent data have now demonstrated a direct link between the molecular chaperone Hsp90 and survivin, a dual regulator of cell proliferation and cell death over-expressed in virtually every human tumor. While the survivin-Hsp90 association may help tumor cells elevate their anti-apoptotic threshold and promote their proliferation, it may also provide new opportunities for rational cancer therapy.
Altieri
Dario C
DC
Department of Cancer Biology and the Cancer Center, University of Massachusetts Medical School, 364 Plantation Street, LRB-428, Worcester, Massachusetts 01605, USA. dario.altieri@umassmed.edu
D000818:Animals; D017209:Apoptosis; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D009363:Neoplasm Proteins; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology*; D011485:Protein Binding; D000077022:Survivin
C107489:BIRC5 protein, human; D018841:HSP90 Heat-Shock Proteins; D051034:Inhibitor of Apoptosis Proteins; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D000077022:Survivin