Fig. 9

HSP90 expression is significantly linked to PUS7 and LASP1 expression in human CRC. a Selected IHC staining images for the expression of HSP90, PUS7, and LASP1 in CRC paired tissues and the respective correlation analysis. b IHC score for HSP90, PUS7, and LASP1 in CRC paired tissues and corresponding Kaplan-Meier plotter. c Correlation analysis among HSP90, PUS7, and LASP1 in a cohort. d Statistical analysis of CRC tissues under diverse staining conditions in a cohort. e Kaplan-Meier analysis based on the HSP90, PUS7, and LASP1 expression. f A schematic model of the role of the HSP90-PUS7-LASP1 axis in CRC metastasis. HSP90 is a novel binding partner of PUS7 and increases PUS7 abundance via the inhibition of the proteasome-mediated degradation of PUS7 in CRC cells. Upregulated PUS7 markedly enhances CRC cell migration and invasion abilities via the regulation of LASP1 in a catalytically independent manner. Of note, PUS7 inhibition in combination with HSP90 inhibitors (NMS-E973) displays superior anti-metastatic activity in CRC