Identification of Genes Regulated by Protoelysis
Abstract
Substrate selection in ubiquitination reactions is achieved by ubiquitin ligases, which simultaneously bind both the target protein and a ubiquitin conjugating enzyme. While recent data indicates that there are a large number of distinct ubiquitin ligases that are responsible for the destruction of hundreds or perhaps thousands of proteins, there are currently no general methods to identify proteins whose levels are controlled by this mechanism. The development of general methods to systematically identify proteins whose abundance is regulated has major implications for: (1) elucidating proteolytic components of signaling pathways such as those activated in response to oncogenes and growth inhibitory factors, (2) identifying candidate drug targets whose altered destruction leads to therapeutic benefit, and (3) identifying genes that are required for the proper destruction of particular proteins of interest. We propose to merge our expertise in gene discovery approaches in yeast and mammalian cells with our experience in the molecular biology of regulated proteolysis to devise techniques that will facilitate the systematic identification of proteins derived from breast cell cDNA libraries whose levels are regulated.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2003
- Accession Number
- ADA417074
Entities
People
- Jeffrey W. Harper
Organizations
- Baylor College of Medicine