Analysis BAP-1 as a Ubiquitin Hydrolase in the BRCA1 Pathway
Abstract
The recurrent theme that has emerged from the structural study of proteins involved in signal transduction and transcriptional regulation is that multiple independently folded globular domains in these proteins often cooperate in macromolecular recognition. These domains are often recognizable by conserved signature amino acid sequence motifs and their spatial organization within a novel protein is often the first clue to its biochemical function. In this aspect, we have identified a novel, nuclear-localized ubiquitin carboxy-terminal hydrolase, BAP-1, that specifically interacts with the RING finger of BRCA1 but not naturally occurring mutants. We are currently investigating the biological consequences of restoring wild-type levels of HP1 in these breast cancer cell lines.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 01, 1999
- Accession Number
- ADA387281
Entities
People
- David C. Schultz
Organizations
- Wistar Institute