STRUCTURAL ANALYSIS OF PROTEIN COMPLEXES IN E3 LIGASE COMPLEX ASSEMBLY

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。 细胞中特定蛋白的多泛素化涉及到E1、5、E2和E3酶的协同作用。Siah1是多蛋白E3泛素连接酶复合体的中心成分，该复合体针对β-连环蛋白而破坏P53的激活。E3复合体除了Siah1外，还包括Siah相互作用蛋白(SIP)、接头蛋白Skp1和F-box蛋白Ebi。

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. Polyubiquitination of specific proteins in cells involves the concerted action of E1,5 E2, and E3 enzymes. Siah1 is the central component of a multiprotein E3 ubiquitin ligase complex that targets Beta-catenin for destruction in response to p53 activation. The E3 complex comprises, in addition to Siah1, Siah-interacting protein (SIP), the adaptor protein Skp1, and the F-box protein Ebi.