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

Oncogene. 1998 Mar 5;16(9):1097-112. doi: 10.1038/sj.onc.1201861.

D E Jensen ¹, 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

Affiliations

Affiliation

1 The Wistar Institute, Philadelphia, Pennsylvania 19104, USA.

PMID: 9528852 DOI: 10.1038/sj.onc.1201861

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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