Rxivist logo

Pyruvate Kinase M Links Glucose Availability to Protein Synthesis

By Nevraj S. Kejiou, Lena Ilan, Stefan Aigner, Enching Luo, Ines Rabano, Nishani Rajakulendran, Hamed S. Najafabadi, St├ęphane Angers, Gene W Yeo, Alexander F Palazzo

Posted 25 Jul 2019
bioRxiv DOI: 10.1101/715086

How human cells coordinate various metabolic processes, such as glycolysis and protein translation, remains unclear. One key insight is that various metabolic enzymes have been found to associate with mRNAs, however whether these enzymes regulate mRNA biology in response to changes in cellular metabolic state remains unknown. Here we report that the glycolytic enzyme, pyruvate kinase M (PKM), inhibits the translation of 7% of the transcriptome in response to elevated levels of glucose and pyruvate. Our data suggest that in the presence of glucose and pyruvate, PKM associates with ribosomes that are synthesizing stretches of polyacidic nascent polypeptides and stalls the elongation step of translation. PKM-regulated mRNAs encode proteins required for the cell cycle and may explain previous results linking PKM to cell cycle regulation. Our study uncovers an unappreciated link between glycolysis and the ribosome that likely coordinates the intake of glycolytic metabolites with the regulation of protein synthesis and the cell cycle.

Download data

  • Downloaded 440 times
  • Download rankings, all-time:
    • Site-wide: 36,162 out of 88,669
    • In molecular biology: 1,185 out of 2,991
  • Year to date:
    • Site-wide: 23,923 out of 88,669
  • Since beginning of last month:
    • Site-wide: 15,967 out of 88,669

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News