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Fig. 4 | Cell Division

Fig. 4

From: Mechanisms for the temporal regulation of substrate ubiquitination by the anaphase-promoting complex/cyclosome

Fig. 4

Different modes of binding of UBE2C and UBE2S to APC/C and effects on ubiquitination of the substrates. Upon engagement of the coactivator (purple) bound to the substrate (shown as a solid red line, with D- and KEN-boxes), UBE2C interacts with APC11 and the WHB domain of APC2 interacts with the backside of UBE2C. This arrangement restricts the sample space that can be explored by UBE2C and allows only a few ubiquitin molecules to be attached to the substrates. UBE2S interacts with a different region of APC11 that is away from the RING domain, while the C-terminal peptide of UBE2S binds to a site between APC2 and APC4 via a flexible linker. The RING domain of APC11 interacts with the acceptor ubiquitin (yellow) on the substrate and presents its K11 residue for accepting a ubiquitin (orange) from UBE2S. Flexible linkers of APC11 and UBE2S are shown by dashed lines

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