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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 journalArticlepeer-review

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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