STRUCTURAL ANALYSIS OF PROTEIN COMPLEXES IN E3 LIGASE COMPLEX ASSEMBLY

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 细胞中特定蛋白质的多泛素化涉及E1、E2和E3酶的协同作用。Siah 1是多蛋白E3泛素连接酶复合物的中心组分，其靶向β-连环蛋白以响应于p53活化而破坏。除了Siah 1之外，E3复合物还包含Siah相互作用蛋白（SIP）、衔接蛋白Skp 1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.