TRIAD1 is negatively regulated by the MDM2 E3 ligase

  • Authors:
    • Seunghee Bae
    • Jin Hyuk Jung
    • In-Sook An
    • Ok-Yeoun Kim
    • Myoung Joo Lee
    • Jae Ho Lee
    • In-Chul Park
    • Su-Jae Lee
    • Sungkwan An
  • View Affiliations

  • Published online on: August 31, 2012     https://doi.org/10.3892/or.2012.2005
  • Pages: 1924-1928
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Abstract

Two RING fingers and DRIL1 (TRIAD1) is a proapoptotic protein that promotes p53 activation in several cancer cell lines, including MCF7, U2OS and A549 cells. In this study, we demonstrated that TRIAD1 is a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). TRIAD1 was found to interact with and be ubiquitinated by MDM2. RNA interference against MDM2 increased endogenous TRIAD1 protein stability. The functional study results suggested that TRIAD1 degradation by MDM2 suppresses TRIAD1-mediated cell growth. These data suggested a novel negative regulatory mechanism of TRIAD1 via MDM2 E3 ligase ubiquitination.
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November 2012
Volume 28 Issue 5

Print ISSN: 1021-335X
Online ISSN:1791-2431

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Spandidos Publications style
Bae S, Jung JH, An I, Kim O, Lee MJ, Lee JH, Park I, Lee S and An S: TRIAD1 is negatively regulated by the MDM2 E3 ligase. Oncol Rep 28: 1924-1928, 2012
APA
Bae, S., Jung, J.H., An, I., Kim, O., Lee, M.J., Lee, J.H. ... An, S. (2012). TRIAD1 is negatively regulated by the MDM2 E3 ligase. Oncology Reports, 28, 1924-1928. https://doi.org/10.3892/or.2012.2005
MLA
Bae, S., Jung, J. H., An, I., Kim, O., Lee, M. J., Lee, J. H., Park, I., Lee, S., An, S."TRIAD1 is negatively regulated by the MDM2 E3 ligase". Oncology Reports 28.5 (2012): 1924-1928.
Chicago
Bae, S., Jung, J. H., An, I., Kim, O., Lee, M. J., Lee, J. H., Park, I., Lee, S., An, S."TRIAD1 is negatively regulated by the MDM2 E3 ligase". Oncology Reports 28, no. 5 (2012): 1924-1928. https://doi.org/10.3892/or.2012.2005