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Posing the APC/C E3 ubiquitin ligase to orchestrate cell division.

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Watson, E. R., Brown, N. G., Peters, J. M., Stark, H., & Schulman, B. A. (2019). Posing the APC/C E3 ubiquitin ligase to orchestrate cell division. Trends in Cell Biology, 29(2), 117-134. doi:10.1016/j.tcb.2018.09.007.


Cite as: http://hdl.handle.net/21.11116/0000-0002-9889-8
Abstract
The anaphase promoting complex/cyclosome (APC/C) E3 ligase controls mitosis and nonmitotic pathways through interactions with proteins that coordinate ubiquitylation. Since the discovery that the catalytic subunits of APC/C are conformationally dynamic cullin and RING proteins, many unexpected and intricate regulatory mechanisms have emerged. Here, we review structural knowledge of this regulation, focusing on: (i) coactivators, E2 ubiquitin (Ub)-conjugating enzymes, and inhibitors engage or influence multiple sites on APC/C including the cullin-RING catalytic core; and (ii) the outcomes of these interactions rely on mobility of coactivators and cullin-RING domains, which permits distinct conformations specifying different functions. Thus, APC/C is not simply an interaction hub, but is instead a dynamic, multifunctional molecular machine whose structure is remodeled by binding partners to achieve temporal ubiquitylation regulating cell division.