This table summarizes the structures of cullin-RING ligase subunits, complexes, substrates, and regulators. It includes structural studies of various components involved in ubiquitin-mediated proteolysis. The table references several studies that provide insights into the molecular architecture of these proteins and their interactions. For example, the structure of the β-TrCP1-Skp1-β-catenin complex is described, revealing details about the SCFβ-TrCP1 ubiquitin ligase. The VHL-ElonginC-ElonginB complex is also analyzed, offering insights into the function of the VHL tumor suppressor. The structure of yeast elongin C in complex with a von Hippel-Lindau peptide is discussed, highlighting its stabilization mechanism. The recognition of hydroxyproline in HIF-1α by pVHL is explored, as well as the structure of the HIF-1α-pVHL complex. The BTB/POZ domain of the promyelocytic leukemia zinc finger oncoprotein is studied, as is the mechanism of SMRT corepressor recruitment by the BCL6 BTB domain. The crystal structure of the BTB domain from PLZF is also presented. Additionally, the structures of ubiquitin and its conjugates, including tetraubiquitin, diubiquitin, and NEDD8, are described, along with their interactions with other proteins. The structure of the APPBP1-UBA3-NEDD8-ATP complex is analyzed, providing insights into the activation of ubiquitin-like proteins. Finally, the structure of the NEDD8 activating enzyme is discussed, offering insights into the ubiquitin transfer cascade. These studies collectively contribute to the understanding of the structural basis of cullin-RING ligase systems and their regulatory mechanisms.This table summarizes the structures of cullin-RING ligase subunits, complexes, substrates, and regulators. It includes structural studies of various components involved in ubiquitin-mediated proteolysis. The table references several studies that provide insights into the molecular architecture of these proteins and their interactions. For example, the structure of the β-TrCP1-Skp1-β-catenin complex is described, revealing details about the SCFβ-TrCP1 ubiquitin ligase. The VHL-ElonginC-ElonginB complex is also analyzed, offering insights into the function of the VHL tumor suppressor. The structure of yeast elongin C in complex with a von Hippel-Lindau peptide is discussed, highlighting its stabilization mechanism. The recognition of hydroxyproline in HIF-1α by pVHL is explored, as well as the structure of the HIF-1α-pVHL complex. The BTB/POZ domain of the promyelocytic leukemia zinc finger oncoprotein is studied, as is the mechanism of SMRT corepressor recruitment by the BCL6 BTB domain. The crystal structure of the BTB domain from PLZF is also presented. Additionally, the structures of ubiquitin and its conjugates, including tetraubiquitin, diubiquitin, and NEDD8, are described, along with their interactions with other proteins. The structure of the APPBP1-UBA3-NEDD8-ATP complex is analyzed, providing insights into the activation of ubiquitin-like proteins. Finally, the structure of the NEDD8 activating enzyme is discussed, offering insights into the ubiquitin transfer cascade. These studies collectively contribute to the understanding of the structural basis of cullin-RING ligase systems and their regulatory mechanisms.