Degradation of activated K-ras orthologue via K-ras-specific lysine residues is required for cytokinesis

Kazutaka Sumita, Hirofumi Yoshino, Mika Sasaki, Nazanin Majd, Emily Rose Kahoud, Hidenori Takahashi, Koh Takeuchi, Taruho Kuroda, Susan Lee, Pascale G. Charest, Kosuke Takeda, John M. Asara, Richard A. Firtel, Dimitrios Anastasiou, Atsuo T. Sasaki

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Background: Targeting oncogenic K-Ras for cancer therapy has remained challenging. Results: Ubiquitination specifically occurs on the activated K-Ras orthologue in Dictyostelium via evolutionary conserved K-Ras lysines, which promotes K-Ras protein degradation. Conclusion: Our results indicate the existence of GTP-loaded K-Ras orthologue-specific degradation system in Dictyostelium. Significance: This work reveals a novel negative feedback regulation for the K-Ras isoform, which is critical for cytokinesis in Dictyostelium.

Original languageEnglish (US)
Pages (from-to)3950-3959
Number of pages10
JournalJournal of Biological Chemistry
Volume289
Issue number7
DOIs
StatePublished - Feb 14 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Sumita, K., Yoshino, H., Sasaki, M., Majd, N., Kahoud, E. R., Takahashi, H., Takeuchi, K., Kuroda, T., Lee, S., Charest, P. G., Takeda, K., Asara, J. M., Firtel, R. A., Anastasiou, D., & Sasaki, A. T. (2014). Degradation of activated K-ras orthologue via K-ras-specific lysine residues is required for cytokinesis. Journal of Biological Chemistry, 289(7), 3950-3959. https://doi.org/10.1074/jbc.M113.531178