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

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

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
Volume415
Issue number4
DOIs
Publication statusPublished - 2011 Dec 2

Fingerprint

Cullin Proteins
Ubiquitin-Protein Ligases
Breast Neoplasms
Neoplasm Metastasis
Proteins
Genes
Cells
Substrates
Tumor Suppressor Proteins
Cullin 1
Carcinogenesis

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kim, Bogyou ; Nam, Hye Jin ; Pyo, Ki Eun ; Jang, Min Jung ; Kim, Ik Soo ; Kim, Dongha ; Boo, Kyungjin ; Lee, Seung Hoon ; Yoon, Jong-Bok ; Baek, Sung Hee ; Kim, Jung Hwa. / Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex. In: Biochemical and Biophysical Research Communications. 2011 ; Vol. 415, No. 4. pp. 720-726.
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Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex. / Kim, Bogyou; Nam, Hye Jin; Pyo, Ki Eun; Jang, Min Jung; Kim, Ik Soo; Kim, Dongha; Boo, Kyungjin; Lee, Seung Hoon; Yoon, Jong-Bok; Baek, Sung Hee; Kim, Jung Hwa.

In: Biochemical and Biophysical Research Communications, Vol. 415, No. 4, 02.12.2011, p. 720-726.

Research output: Contribution to journalArticle

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AU - Kim, Bogyou

AU - Nam, Hye Jin

AU - Pyo, Ki Eun

AU - Jang, Min Jung

AU - Kim, Ik Soo

AU - Kim, Dongha

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AU - Lee, Seung Hoon

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AU - Baek, Sung Hee

AU - Kim, Jung Hwa

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