Breast Cancer Metastasis Suppressor 1 (Brms1) is Stabilized by the Hsp90 Chaperone.
From: Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, USA.
Biochemical and biophysical research communications
- Publish Date: Oct 2006
- ISSN: 0006-291X
- Volume: 348
- Issue: 4
- Pages: 1429-35
- Medium: Print
- Language: English
- Citation (JAMA): Hurst Douglas R, Mehta Alka, Moore Blake P, et al. Breast Cancer Metastasis Suppressor 1 (Brms1) is Stabilized by the Hsp90 Chaperone.. Biochem. Biophys. Res. Commun. Oct 2006;348:1429-35
Abstract
Breast cancer metastasis suppressor 1 (BRMS1) is a member of the mSin3-HDAC transcription co-repressor complex. However, the proteins associated with BRMS1 have not been fully identified. Yeast two-hybrid screen, immuno-affinity chromatography, and co-immunoprecipitation experiments were performed to identify BRMS1 interacting proteins (BIPs). In addition to known core mSin3 transcriptional complex components RBBP1 and mSDS3, BRMS1 interacted with other proteins including three chaperones: DNAJB6 (MRJ), Hsp90, and Hsp70. Hsp90 is a known target of HDAC6 and reversible acetylation is one of the mechanisms that is implicated in regulation of Hsp90 chaperone complex activity. BRMS1 interacted with class II HDACs, HDAC 4, 5, and 6. We further found that BRMS1 is stabilized by Hsp90, and its turnover is proteasome dependent. The stability of BRMS1 protein may be important in maintaining the functional role of BRMS1 in metastasis suppression.
Mesh Headings (Keywords): Animals, COS Cells, Cercopithecus aethiops, HSP90 Heat-Shock Proteins, Histone Deacetylases, Humans, Immunoprecipitation, Neoplasm Proteins, Two-Hybrid System Techniques
Check for Full Text / PubMed Unique Identifier (PMID): 16919237
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