Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex

Bogyou Kim, Hye Jin Nam, Ki Eun Pyo, Min Jung Jang, Ik Soo Kim, Dongha Kim, Kyungjin Boo, Seung Hoon Lee, Jong Bok Yoon, Sung Hee Baek, Jung Hwa Kim

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47 Citations (Scopus)


Breast cancer metastasis suppressor 1 (BRMS1) suppresses metastasis without affecting primary tumorigenesis. The regulatory mechanism of BRMS1 at the protein level has not been revealed until recently. Here, we found that cullin 3 (Cul3), a component of E3 ubiquitin ligase, is a new binding partner of BRMS1 and the interaction between BRMS1 and Cul3 is mediated by the SPOP adaptor protein. Intriguingly, BRMS1 turns out to be a potent substrate that is ubiquitinated by the Cul3-SPOP complex. Knockdown of SPOP increases the level of BRMS1 protein and represses the expression of BRMS1 repressive target genes such as OPN and uPA in breast cancer cells. These results suggest that the novel regulatory mechanism of BRMS1 by Cul3-SPOP complex is important for breast cancer progression.

Original languageEnglish
Pages (from-to)720-726
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 2011 Dec 2

Bibliographical note

Funding Information:
This work was supported by the Korea Science and Engineering Foundation (KOSEF) Grant funded by the Korea Government (MEST; 531-2008-1-C00043 , 2009-0064577 , and 2008-0060604 ) to J.H.K.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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