MOLECULAR LOGIC OF SUBSTRATE RECOGNITION BY THE CULLIN-4 UBIQUITIN LIGASE

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。所列机构为中心机构，不一定为研究者机构。基于Cullin的泛素连接酶是E3连接酶的最大家族。在人类中有7种Cullin，每种Cullin都利用不同的底物特异性受体家族来将底物募集到泛素化机制中。尽管大多数Cullin的底物特异性受体家族是已知的，但Cullin-4家族的该家族的身份仍然难以捉摸。使用来自人细胞的Cullin-4和DDB 1蛋白复合物的串联亲和纯化和质谱，我们将尝试1）鉴定和2）表征Cullin-4的底物特异性受体家族。

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. Cullin based ubiquitin ligases are the largest family of E3 ligases. There is 7 Cullins in humans and every Cullin utilizes a different family of substrate specific receptors in order to recruit the substrate to the ubiquitination machinery. Although the family of substrate specific receptors are known for most of the Cullins, the identity of this family for the Cullin-4 family remains elusive. Using tandem-affinity purification of Cullin-4 and DDB1 protein complexes from human cells and mass spectrometry we will attempt to 1) identify and 2) characterize the family of substrate-specirfic receptors for Cullin-4.