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

doi:10.1016/j.bbrc.2011.10.154

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

Department of Anatomy

Research output: Contribution to journal › Article › peer-review

53 Scopus citations

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 language	English
Pages (from-to)	720-726
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	415
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2011.10.154
State	Published - 2 Dec 2011

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.

Keywords

Breast cancer cells
BRMS1
Cul3
SPOP
Ubiquitination

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bbrc.2011.10.154

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

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.",

keywords = "Breast cancer cells, BRMS1, Cul3, SPOP, Ubiquitination",

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

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.",

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AU - Kim, Bogyou

AU - Nam, Hye Jin

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AU - Jang, Min Jung

AU - Kim, Ik Soo

AU - Kim, Dongha

AU - Boo, Kyungjin

AU - Lee, Seung Hoon

AU - Yoon, Jong Bok

AU - Baek, Sung Hee

AU - Kim, Jung Hwa

N1 - 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.

PY - 2011/12/2

Y1 - 2011/12/2

N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Keywords

UN SDGs

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