HYSK1 promotes cancer cell proliferation and migration through negative regulation of p16^INK4a under hypoxic conditions.

ABSTRACT: The alteration of expression of p16^INK4a, a well-known cyclin-dependent kinase inhibitor involved in cell cycle control, in tumors is unclear, especially under hypoxic conditions. To evaluate p16^INK4a regulation, we performed a protein microarray analysis. Among 1,800 proteins in the array, we identified hYSK1 as a novel protein that interacts with the tumor suppressor p16^INK4a. hYSK1, a member of the Ste20 family of serine/threonine protein kinases, promotes cell migration and tumorigenesis and is activated by oxidative stress. However, the molecular mechanisms underlying the oncogenic potential of hYSK1 remain elusive. Here, we report that hYSK1 interacts with p16^INK4a under hypoxic conditions in tumors, where it negatively regulates p16^IN

SUBMITTER: Lee MH 

PROVIDER: S-EPMC5687670 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature