[PDF][PDF] A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression

WC Yuan, YR Lee, SF Huang, YM Lin, TY Chen… - Cancer cell, 2011 - cell.com
WC Yuan, YR Lee, SF Huang, YM Lin, TY Chen, HC Chung, CH Tsai, HY Chen, CT Chiang…
Cancer cell, 2011cell.com
Tumor hypoxia is associated with disease progression and treatment failure, but the hypoxia
signaling mechanism is not fully understood. Here, we show that KLHL20, a Cullin3 (Cul3)
substrate adaptor induced by HIF-1, coordinates with the actions of CDK1/2 and Pin1 to
mediate hypoxia-induced PML proteasomal degradation. Furthermore, this PML destruction
pathway participates in a feedback mechanism to maximize HIF-1α induction, thereby
potentiating multiple tumor hypoxia responses, including metabolic reprogramming …
Summary
Tumor hypoxia is associated with disease progression and treatment failure, but the hypoxia signaling mechanism is not fully understood. Here, we show that KLHL20, a Cullin3 (Cul3) substrate adaptor induced by HIF-1, coordinates with the actions of CDK1/2 and Pin1 to mediate hypoxia-induced PML proteasomal degradation. Furthermore, this PML destruction pathway participates in a feedback mechanism to maximize HIF-1α induction, thereby potentiating multiple tumor hypoxia responses, including metabolic reprogramming, epithelial-mesenchymal transition, migration, tumor growth, angiogenesis, and chemoresistance. In human prostate cancer, overexpression of HIF-1α, KLHL20, and Pin1 correlates with PML down-regulation, and hyperactivation of the PML destruction pathway is associated with disease progression. Our study indicates that the KLHL20-mediated PML degradation and HIF-1α autoregulation play key roles in tumor progression.
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