This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Post-translational covalent attachment of ubiquitin and ubiquitin-like proteins has emerged as a predominant cellular regulatory mechanism, with important roles in controlling cell division, signal transduction, embryonic development, endocytic trafficking and the immune response. As a result, deregulation of the pathways for attaching ubiquitin-like modifications plays a role in a number of diseases, including cancer, birth defects and Parkinson s Disease, and several viruses hijack these pathways during infection. Ubiquitin-like proteins function by remodelling the surface of their target proteins, changing their target s half-life, enzymatic activity, protein/protein interactions, subcellular localization or other properties. We are trying to understand the mechanisms of enzymes that tag protein substrates with ubiquitin and ubiquitin-like proteins. In addition to our efforts to understand the basic principles governing ubiquitin-like protein transfer, we are studying the structures of proteins involved in the ubiquitin pathway that play a role in childhood cancers treated at St. Jude Children s Research Hospital.
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