Due to necessary maintenance, Xenbase will be unavailable from December 24-29, 2014. We apologize for the inconvenience.

Click on this message to dismiss it.
Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-37930
Cell. May 16, 2008; 133 (4): 653-65.

Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex.

Jin L , Williamson A , Banerjee S , Philipp I , Rape M .


Abstract
The anaphase-promoting complex (APC/C) orchestrates progression through mitosis by decorating cell-cycle regulators with ubiquitin chains. To nucleate chains, the APC/C links ubiquitin to a lysine in substrates, but to elongate chains it modifies lysine residues in attached ubiquitin moieties. The mechanism enabling the APC/C, and ubiquitin ligases in general, to switch from lysine residues in substrates to specific ones in ubiquitin remains poorly understood. Here, we determine the topology and the mechanism of assembly for the ubiquitin chains mediating functions of the human APC/C. We find that the APC/C triggers substrate degradation by assembling K11-linked ubiquitin chains, the efficient formation of which depends on a surface of ubiquitin, the TEK-box. Strikingly, homologous TEK-boxes are found in APC/C substrates, where they facilitate chain nucleation. We propose that recognition of similar motifs in substrates and ubiquitin enables the APC/C to assemble ubiquitin chains with the specificity and efficiency required for tight cell-cycle control.

PubMed ID: 18485873
PMC ID: PMC2696189
Article link: Cell.
Grant support: DP2 OD003088-01 NCCDPHP CDC HHS, R01 GM083064-01 NIGMS NIH HHS , DP2 OD003088-01 NIH HHS , DP2 OD003088-01 NIH HHS

Genes referenced: tek
Antibodies referenced:
Morpholinos referenced:

My Xenbase: [ Log-in / Register ]
version: [3.3]


Major funding for Xenbase is provided by the National Institute of Child Health and Human Development, grant P41 HD064556