Polo-like kinase 1 coordinates biosynthesis during cell cycle progression by directly activating pentose phosphate pathway

Nat Commun. 2017 Nov 15;8(1):1506. doi: 10.1038/s41467-017-01647-5.

Abstract

Two hallmarks for cancer cells are the accelerated cell cycle progression as well as the altered metabolism, however, how these changes are coordinated to optimize the growth advantage for cancer cells are still poorly understood. Here we identify that Polo-like kinase 1 (Plk1), a key regulator for cell mitosis, plays a critical role for biosynthesis in cancer cells through activating pentose phosphate pathway (PPP). We find that Plk1 interacts with and directly phosphorylates glucose-6-phosphate dehydrogenase (G6PD). By activating G6PD through promoting the formation of its active dimer, Plk1 increases PPP flux and directs glucose to the synthesis of macromolecules. Importantly, we further demonstrate that Plk1-mediated activation of G6PD is critical for its role to promote cell cycle progression and cancer cell growth. Collectively, these findings establish a critical role for Plk1 in regulating biosynthesis in cancer cells, exemplifying how cell cycle progression and metabolic reprogramming are coordinated for cancer progression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Cycle*
  • Cell Line, Tumor
  • Female
  • Glucose / metabolism*
  • Glucosephosphate Dehydrogenase / metabolism
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Male
  • Mice, Inbred BALB C
  • Mice, Nude
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Neoplasms / pathology
  • Pentose Phosphate Pathway*
  • Polo-Like Kinase 1
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Transplantation, Heterologous

Substances

  • Cell Cycle Proteins
  • Proto-Oncogene Proteins
  • Glucosephosphate Dehydrogenase
  • Protein Serine-Threonine Kinases
  • Glucose