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. Cullins (Cul) are components of SCF-type ubiquitin ligases implicated in signal transduction, cell cycle control, and differentiation. These diverse functions are thought to be mediated by ubiquitin-dependent destruction of critical regulatory proteins. While there is a plethora of information on Cul-1, very little is known about its family members. The primary focus of this project involves identifying interacting proteins of Cul-3 and Cul-4. It is also interesting to point out that these proteins have been implicated in disease and are required for murine viability. Because these proteins are conserved in yeast (pcu3 and pcu4), we have chosen it as a platform in order to carry out the purification of the endogenous complex. We have employed the tandem affinity purification method for both pcu3 and pcu4 and have been recently successful in obtaining unique bands for both proteins.
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