The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Breast Cancer Metastasis Suppressor 1 (BRMS1) Forms Complexes with Retinoblastoma-binding Protein 1 (RBP1) and the mSin3 Histone Deacetylase Complex and Represses Transcription
Open accessAbstract
Breast cancer metastasis suppressor 1 (BRMS1) suppresses metastasis of multiple human and murine cancer cells without inhibiting tumorigenicity. By yeast two-hybrid and co-immunoprecipitation, BRMS1 interacts with retinoblastoma binding protein 1 and at least seven members of the mSin3 histone deacetylase (HDAC) complex in human breast and melanoma cell lines. BRMS1 co-immunoprecipitates enzymatically active HDAC proteins and represses transcription when recruited to a Gal4 promoter in vivo. BRMS1 exists in large mSin3 complex(es) of approximately 1.4-1.9 MDa, but also forms smaller complexes with HDAC1. Deletion analyses show that the carboxyl-terminal 42 amino acids of BRMS1 are not critical for interaction with much of the mSin3 complex and that BRMS1 appears to have more than one binding point to the complex. These results further show that BRMS1 may participate in transcriptional regulation via interaction with the mSin3.HDAC complex and suggest a novel mechanism by which BRMS1 might suppress cancer metastasis.
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Cites
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Histone deacetylases and cancer: causes and therapies
Marks, P. A., Rifkind, R. A., Richon, V. M., Breslow, R., Miller, T., & Kelly, W. K. (2001) · Nature reviews. Cancer · doi:10.1038/35106079 · Cited by 1,866
Histone-deacetylase inhibitors: novel drugs for the treatment of cancer
Johnstone, R. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd772 · Cited by 1,515
Nuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
Nagy, L., Kao, H.-Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80218-4 · Cited by 1,230
Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (1997) · Cell · doi:10.1016/s0092-8674(00)80216-0 · Cited by 578
Ahringer, J. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02066-7 · Cited by 388
Lechner, T., Carrozza, M. J., Yu, Y., Grant, P. A., Eberharter, A., Vannier, D., Brosch, G., Stillman, D. J., Shore, D., & Workman, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005730200 · Cited by 97
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Cited by
Steeg, P. S. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.25 · Cited by 1,363
Hurst, D. R., Edmonds, M. D., Scott, G. K., Benz, C. C., Vaidya, K. S., & Welch, D. R. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3559 · Cited by 411
Self-citationQuantitation of HDAC1 mRNA Expression in Invasive Carcinoma of the Breast*
Zhang, Z., Yamashita, H., Toyama, T., Sugiura, H., Ando, Y., Mita, K., Hamaguchi, M., Hara, Y., Kobayashi, S., & Iwase, H. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-6001-1 · Cited by 305
Song, W.-M., Agrawal, P., Von Itter, R., Fontanals-Cirera, B., Wang, M., Zhou, X., Mahal, L. K., Hernando, E., & Zhang, B. (2021) · Nature Communications · doi:10.1038/s41467-021-21457-0 · Cited by 62
Metadata
- Authors
- Meehan, W. J., Samant, R. S., Hopper, J. E., Carrozza, M. J., Shevde, L. A., Workman, J. L., Eckert, K. A., Verderame, M. F., & Welch, D. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 2
- Pages
- 1562-1569
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2036362283
- Cited by
- 170
- References
- 7
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Breast Cancer Metastasis Suppressor 1 (BRMS1) Forms Complexes with Retinoblastoma-binding Protein 1 (RBP1) and the mSin3 Histone Deacetylase Complex and Represses Transcription. https://app.cochat.ai/papers/10.1074/jbc.m307969200
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- Meehan, W. J., Samant, R. S., Hopper, J. E., Carrozza, M. J., Shevde, L. A., Workman, J. L., Eckert, K. A., Verderame, M. F., & Welch, D. R. (2004). Breast Cancer Metastasis Suppressor 1 (BRMS1) Forms Complexes with Retinoblastoma-binding Protein 1 (RBP1) and the mSin3 Histone Deacetylase Complex and Represses Transcription. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m307969200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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