Yamano H .

Wellcome Trust , Biotechnology and Biological Sciences Research Council , Medical Research Council , Cancer Research UK, 13586 Cancer Research UK, MR/M010899/1 Medical Research Council

	Figure 1. . Schematic diagrams of RING E3 ubiquitin ligases.RING-type E3 ligases serve as scaffolds to bring together the E2~Ub conjugate and the substrate. E3s play a role in stimulating Ub transfer to the substrate from E2~Ub conjugate. E2-binding RING domain is coloured in light blue. ( A) Monomeric RING E3 ubiquitin ligases (for example, c-Cbl). ( B) A simplified cartoon view of APC/C RING E3 ubiquitin ligase with a co-activator such as Cdc20 and Cdh1. ( C) The APC/C is a multi-subunit cullin-RING E3 ubiquitin ligase that uses two E2s. APC/C, anaphase-promoting complex/cyclosome.
	Figure 2. . APC/C structure and overall organisation.( A) APC/C structure. The image was generated by using the Protein Data Bank file (4UI9). The indicated numbers represent APC/C subunits. ( B) Schematic view of the APC/C structure based on ( A). Left: APC Cdc20; right: APC/C Cdh1. Cdc20 activates the APC/C in metaphase and anaphase to degrade substrates such as cyclin B and securin and then Cdh1 takes over to degrade APC/C substrates in late anaphase and G 1. ( C) The APC/C complex can be divided into three modules: the catalytic module (Apc2-Apc11) that interacts with E2s, the substrate recognition TPR lobe and the scaffolding platform (Apc1-Apc4-Apc5). During the ubiquitylation catalysis, both substrate and E2s are positioned in or near the APC/C central cavity. APC/C, anaphase-promoting complex/cyclosome; TPR, tetratricopeptide repeat.
	Figure 3. . Phosphorylation-dependent activation of the APC/C for APC/C Cdc20.Interphase APC/C is inactive without the recruitment of Cdc20, which is presented from a front view and a back view of the APC/C. The disordered loop domain of Apc1 (Apc1-loop 300), which is located in the N-terminal WD40 domain, blocks Cdc20-NTD access to the APC/C, in particular the C-box–binding sites on Apc8B. Yellow dotted circle highlights the C-box–binding site. In mitosis, Cdk1-cyclinB-Cks phosphorylates the disordered loop domain of Apc3 (Apc3 loop), which allows Cks-bound Cdk1-cyclin B loading to Apc3 loop. Cdk1-cyclinB-Cks then stimulates phosphorylation of Apc1-loop 300 as an intramolecular phosphorylation relay. Upon phosphorylation, inhibitory domain Apc1-loop 300 is dislocated from the C-box–binding site, allowing Cdc20 association, the C-box-dependent activation and subsequent ubiquitylation catalysis (“cartoon view of the APC/C”). The isoleucine-arginine (IR) tail of Cdc20 binds to Apc3 and the C-box interacts with Apc8B for activation of the APC/C. Both IR tail binding and C-box binding ensure stable binding of co-activator (Cdc20) to the APC/C. The WD40 domain of co-activator is responsible for substrate degron recognition. The RING subunit Apc11 is coloured in light blue. APC/C, anaphase-promoting complex/cyclosome.
	Figure 4. . APC/C inhibitors target the APC/C at multiple levels.( A) Overexpression or high dose of the destruction box (D-box) fragment (+op-D-box) competes with substrates to bind to the D-box–binding pocket on the WD40 domain (competitive inhibition). A small-molecule Apcin binds the D-box–binding pocket on the side face of the WD40 domain (+Apcin). ( B) A small-molecule tosyl- l-arginine methyl ester (TAME), which resembles the isoleucine-arginine (IR) tail of Cdc20 and Cdh1, binds APC3 to interfere with the IR tail–binding site (+TAME). EM study suggests that TAME might compete with Cdc20 to bind at the IR tail and the C-box–binding sites. ( C) Emi1 inhibits the APC/C at multiple levels (+Emi1). The D-box (weak) binds the WD40 domain of Cdc20/Cdh1, a zinc-binding region (ZBR) interferes with Ubc2C-dependent APC/C activity and the C-terminal LRRL tail interferes with Ube2S binding to the APC/C. The LRRL tail sequence of Emi1 is identical to the LRRL motif of Ube2S. In vivo target of Emi1 is Cdh1. ( D) The main effector of the spindle assembly checkpoint (SAC) is the mitotic checkpoint complex (MCC), which inhibits the APC/C at multiple levels. In vivo target of MCC is Cdc20. MCC binds both the D-box–binding pocket and the KEN-box–binding surface of the WD40 domain and blocks WD40-mediated substrate binding. MCC also blocks Ube2C-dependent APC/C activity at the closed MCC configuration; however, Ube2S-dependent APC/C activity is not inhibited by MCC. Schematic diagrams are based on the cartoon view of the APC/C in Figure 3 (bottom left). APC/C, anaphase-promoting complex/cyclosome.

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