STHMN1 is a major cytosolic phosphoprotein and a microtubule-depolymerizing molecule involved in the metastatic process of various cancers; however, the mechanism of its regulation has not been fully clarified. The activity of STHMN1 is controlled by PI3K, which requires maintaining a stable microtubule network during migration.6 Phosphorylation of STHMN1 is mediated by a number of protein kinases including p27, an inhibitor of cyclin-dependent kinase complexes. In the absence of PI3K/Akt activity, captured microtubules are progressively broken down and cells lose their ability to follow the chemotactic gradient. The relationship between STHMN1 and p27 was identified in previous studies.19,20 Researchers reported that STHMN1 binds to p27 cells, and that cells with strong STHMN1 expression and weak p27 expression display increased proliferation and invasion capacity in tumor tissue. STMN1 was also shown to be activated by the Ras-mitogen-activated protein kinase and hedgehog signaling pathway in some studies.21 Researchers observed thiostrepton got over to TBR by blocking transition from G1 to S phase in cell lines.22 Treatment with low-dose anti-STHMN1 therapy and taxane was shown to halt tumor invasion in a breast cancer xenograft.23