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BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression.

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.
AuthorsD E Jensen, M Proctor, S T Marquis, H P Gardner, S I Ha, L A Chodosh, A M Ishov, N Tommerup, H Vissing, Y Sekido, J Minna, A Borodovsky, D C Schultz, K D Wilkinson, G G Maul, N Barlev, S L Berger, G C Prendergast, F J Rauscher 3rd
JournalOncogene (Oncogene) Vol. 16 Issue 9 Pg. 1097-112 (Mar 05 1998) ISSN: 0950-9232 [Print] England
PMID9528852 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • BAP1 protein, mouse
  • BRCA1 Protein
  • Carrier Proteins
  • Recombinant Proteins
  • Tumor Suppressor Proteins
  • BARD1 protein, human
  • Bard1 protein, mouse
  • Ubiquitin-Protein Ligases
  • Thiolester Hydrolases
  • Ubiquitin Thiolesterase
Topics
  • Amino Acid Sequence
  • Animals
  • BRCA1 Protein (chemistry, metabolism)
  • Base Sequence
  • Binding Sites
  • Breast Neoplasms (genetics, pathology)
  • Carrier Proteins (biosynthesis, chemistry, 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, chemistry, metabolism)
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Thiolester Hydrolases (chemistry, genetics, metabolism)
  • Transfection
  • Tumor Suppressor Proteins
  • Ubiquitin Thiolesterase
  • Ubiquitin-Protein Ligases
  • Zinc Fingers

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