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PMID:9528852
Citation |
Jensen, DE, Proctor, M, Marquis, ST, Gardner, HP, Ha, SI, Chodosh, LA, Ishov, AM, Tommerup, N, Vissing, H, Sekido, Y, Minna, J, Borodovsky, A, Schultz, DC, Wilkinson, KD, Maul, GG, Barlev, N, Berger, SL, Prendergast, GC and Rauscher, FJ 3rd (1998) BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression. Oncogene 16:1097-112 |
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Abstract |
We have identified a novel protein, BAP1, which binds to the RING finger domain of the Breast/Ovarian Cancer Susceptibility Gene product, BRCA1. BAP1 is a nuclear-localized, ubiquitin carboxy-terminal hydrolase, suggesting that deubiquitinating enzymes may play a role in BRCA1 function. BAP1 binds to the wild-type BRCA1-RING finger, but not to germline mutants of the BRCA1-RING finger found in breast cancer kindreds. BAP1 and BRCA1 are temporally and spatially co-expressed during murine breast development and remodeling, and show overlapping patterns of subnuclear distribution. BAP1 resides on human chromosome 3p21.3; intragenic homozygous rearrangements and deletions of BAP1 have been found in lung carcinoma cell lines. BAP1 enhances BRCA1-mediated inhibition of breast cancer cell growth and is the first nuclear-localized ubiquitin carboxy-terminal hydrolase to be identified. BAP1 may be a new tumor suppressor gene which functions in the BRCA1 growth control pathway. |
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Keywords |
Amino Acid Sequence; Animals; BRCA1 Protein/chemistry; BRCA1 Protein/metabolism; Base Sequence; Binding Sites; Breast Neoplasms/genetics; Breast Neoplasms/pathology; Carrier Proteins/biosynthesis; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cell Division; Chromosome Mapping; Chromosomes, Human, Pair 3; Female; Gene Rearrangement; Homozygote; Humans; Karyotyping; Lung Neoplasms/genetics; Mice; Molecular Sequence Data; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Thiolester Hydrolases/chemistry; Thiolester Hydrolases/genetics; Thiolester Hydrolases/metabolism; Transfection; Tumor Suppressor Proteins; Ubiquitin Thiolesterase; Ubiquitin-Protein Ligases; Zinc Fingers |
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Significance
Annotations
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