Differences in the regulation of K-Ras and H-Ras isoforms by monoubiquitination

Rachael Baker, Emily M. Wilkerson, Kazutaka Sumita, Daniel G. Isom, Atsuo T. Sasaki, Henrik G. Dohlman, Sharon L. Campbell

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

Background: Ras proteins are critical regulators of cellular growth and are differentially modified by ubiquitination. Results: Chemical ubiquitination and immunoprecipitation assays demonstrate that monoubiquitination causes sustained H-Ras activation in the absence of oncogenic mutations. Conclusion: The mechanism by which H-Ras is activated by monoubiquitination is both isoform-specific and site-specific. Significance: Monoubiquitination adds a new level of regulation and complexity to isoform-specific Ras signaling.

Original languageEnglish (US)
Pages (from-to)36856-36862
Number of pages7
JournalJournal of Biological Chemistry
Volume288
Issue number52
DOIs
StatePublished - Dec 27 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Baker, R., Wilkerson, E. M., Sumita, K., Isom, D. G., Sasaki, A. T., Dohlman, H. G., & Campbell, S. L. (2013). Differences in the regulation of K-Ras and H-Ras isoforms by monoubiquitination. Journal of Biological Chemistry, 288(52), 36856-36862. https://doi.org/10.1074/jbc.C113.525691