Detailed Information
Cited 4 time in 
Cited 3 time in 
Cited 3 time in
Metadata Downloads
TRIAD1 is negatively regulated by the MDM2 E3 ligase
- Authors
- Bae, Seunghee; Jung, Jin Hyuk; An, In-Sook; Kim, Ok-Yeoun; Lee, Myoung Joo; Lee, Jae Ho; Park, In-Chul; Lee, Su-Jae; An, Sungkwan
- Issue Date
- Nov-2012
- Publisher
- SPANDIDOS PUBL LTD
- Keywords
- p53; murine double minute 2; ubiquitination; two RING fingers and DRIL1
- Citation
- ONCOLOGY REPORTS, v.28, no.5, pp.1924 - 1928
- Indexed
- SCIE
SCOPUS
- Journal Title
- ONCOLOGY REPORTS
- Volume
- 28
- Number
- 5
- Start Page
- 1924
- End Page
- 1928
- ISSN
- 1021-335X
- 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - 서울 자연과학대학 > 서울 생명과학과 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.