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Updated: May 24, 2026

Microinjection of mRNA and Morpholino Antisense Oligonucleotides in Zebrafish Embryos.
Published on: May 7, 2009
PKM2 enters the morpheein academy
Galina Semenova1, Jonathan Chernoff
1Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA 19111, USA.
The glycolytic enzyme PKM2, in its dimeric form, acts as a protein kinase. It phosphorylates STAT3 in the nucleus, promoting gene expression linked to cell transformation.
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Biology
Background:
- The glycolytic enzyme pyruvate kinase M2 (PKM2) is known to play roles beyond glycolysis.
- Its involvement in nuclear functions and regulation of gene expression is an emerging area of research.
Discussion:
- Gao et al. demonstrate that dimeric PKM2 exhibits protein kinase activity.
- This activity is directed towards STAT3 phosphorylation within the nucleus.
Key Insights:
- Dimeric PKM2 directly phosphorylates STAT3, a key transcription factor.
- This phosphorylation event upregulates the expression of genes associated with cellular transformation.
Outlook:
- This finding reveals a novel mechanism linking glycolysis to cancer progression.
- Targeting PKM2's nuclear kinase activity could offer new therapeutic strategies for cancer treatment.
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