Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex |
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| Authors: | 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 |
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| Institution: | aDepartment of Biological Sciences, Creative Research Initiative Center for Chromatin Dynamics, Seoul National University, Seoul 151-742, South Korea;bDepartment of Biological Sciences, Inha University, Incheon 402-751, South Korea;cDepartment of Biochemistry and Translational Research Center for Protein Function Control, Yonsei University, Seoul 120-749, South Korea |
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| 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. |
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| Keywords: | BRMS1 SPOP Cul3 Ubiquitination Breast cancer cells |
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