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Title: Pyruvate kinase M2 isoform (PKM2) phosphorylating histone


Tools: VMD, 3ds max, Photoshop

Target Audience: Research scientists, investors

Background: This work is highlighting an area of research in regards to pyruvate kinase M2 isoform (PKM2), generated from alternative splicing of the PKM gene. PKM2 expresses the 56 amino acid exon 10, while PKM1 expresses the 56 amino acid exon 9. The difference between these exons is restricted to 22 unique amino acid residues. The unique region within exon 10 imparts a different functionality to the enzyme that includes being a transcriptional coactivator and tending to form dimers rather than tetramers. PKM2’s role in histone modification that leads to epigenetic change in gene expression and tumorigenesis is exemplified in a recent study published by Yang et al. where it was shown that PKM2 directly interacts with histone H3, phosphorylating it at threonine 11.

VIZBI conference: I had the pleasure of attending VIZBI 2015 conference in Cambridge, MA. I presented my poster about how Visual Molecular Dynamic (VMD) is used to ensure structural and size relationship accuracy in my molecular illustrations and animation. I also get to meet John Stone, the scientist/programmer behind VMD.

Process works:

Storyboards: I chose the do full render of the second panel since it tells the key point of the Yang et al paper.


Process works:

Import PKM2 (3BJF) from Protein Data Bank to VMD


Iqbal, M. A., Gupta, V., Gopinath, P., Mazurek, S., & Bamezai, R. N. (2014). Pyruvate kinase M2 and cancer: An updated assessment. FEBS Letters, 588(16), 2685-2692. 

Li, Z., Yang, P., & Li, Z. (2014). The multifaceted regulation and functions of PKM2 in tumor progression. Biochimica Et Biophysica Acta, 1846(2), 285-296. 

Yang, W., Xia, Y., Hawke, D., Li, X., Liang, J., Xing, D., et al. (2012). PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. Cell, 150(4), 685-696.

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