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

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 基于库林的泛素连接酶是E3连接酶中最大的家族。在人类中有7个库林，每个库林利用一个 不同的底物特异性受体家族，以便将底物招募到泛素化机制。虽然 底物特异性受体家族是大多数cullin家族的已知成员，这个家族的身份是cullin-4家族。 仍然难以捉摸。串联亲和层析纯化人细胞和群体中的cullin-4和DDB1蛋白复合体 光谱分析我们将尝试1)鉴定和2)鉴定库林-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.