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. Conjugation of ubiquitin or one of the many ubiquitin-like proteins to a substrate is an important regulatory mechanism for many cellular processes. The process for attaching ubiquitin or an ubiquitin-like molecule to a protein substrate utilizes at least three distinct steps. First ubiquitin is activated and attached to the active-site cysteine of the E1 ubiquitin-activating enzyme, next the ubiquitin is transferred to the active-site cysteine of an E2 ubiquitin-conjugating enzyme. For the class of RING domain containing E3 ubiquitin ligases the final step is mediated by the RING domain which associates with the E2 and somehow facilitates the transfer of ubiquitin to the substrate. Our laboratory is interested in understanding the interaction of E2 and E3 enzymes. We have identified an interaction between the E2 Ubc9 and a RING containing protein of unknown function. However, this interaction is weak when test with purified components. We are searching for accessory proteins that may facilitate this interaction in vivo.
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