The non-apoptotic function of Caspase-8 in negatively regulating the CDK9-mediated Ser2 phosphorylation of RNA polymerase II in cervical cancer

Cell Mol Life Sci. 2022 Nov 18;79(12):597. doi: 10.1007/s00018-022-04598-3.

Abstract

Cervical cancer is the fourth most frequently diagnosed and fatal gynecological cancer. 15-61% of all cases metastasize and develop chemoresistance, reducing the 5-year survival of cervical cancer patients to as low as 17%. Therefore, unraveling the mechanisms contributing to metastasis is critical in developing better-targeted therapies against it. Here, we have identified a novel mechanism where nuclear Caspase-8 directly interacts with and inhibits the activity of CDK9, thereby modulating RNAPII-mediated global transcription, including those of cell-migration- and cell-invasion-associated genes. Crucially, low Caspase-8 expression in cervical cancer patients leads to poor prognosis, higher CDK9 phosphorylation at Thr186, and increased RNAPII activity in cervical cancer cell lines and patient biopsies. Caspase-8 knock-out cells were also more resistant to the small-molecule CDK9 inhibitor BAY1251152 in both 2D- and 3D-culture conditions. Combining BAY1251152 with Cisplatin synergistically overcame chemoresistance of Caspase-8-deficient cervical cancer cells. Therefore, Caspase-8 expression could be a marker in chemoresistant cervical tumors, suggesting CDK9 inhibitor treatment for their sensitization to Cisplatin-based chemotherapy.

Keywords: CDK9; Caspase-8; Non-apoptotic function; P-TEFb; RNAPII; Transcription.

MeSH terms

  • Caspase 8 / genetics
  • Caspase 8 / metabolism
  • Cisplatin / pharmacology
  • Cyclin-Dependent Kinase 9 / genetics
  • Cyclin-Dependent Kinase 9 / metabolism
  • Female
  • Humans
  • Phosphorylation
  • Protein Kinase Inhibitors
  • RNA Polymerase II* / metabolism
  • Uterine Cervical Neoplasms* / drug therapy
  • Uterine Cervical Neoplasms* / genetics

Substances

  • RNA Polymerase II
  • Caspase 8
  • Cisplatin
  • Protein Kinase Inhibitors
  • CDK9 protein, human
  • Cyclin-Dependent Kinase 9