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Structural biology

A new look for the APC

Nature volume 470, pages 182–183 (2011)Cite this article

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Solving the structure of protein complexes is particularly challenging when they contain many subunits. In the case of the APC, a fruitful strategy has been to gain information by subtracting subunits. See Article p.227 and Letter p.274

Many cell-cycle regulators are targeted for degradation by being tagged with chains of the small protein ubiquitin. Ubiquitin ligase enzymes mediate the selection of target proteins. One of the most complex ubiquitin ligases is the anaphase-promoting complex (APC) — a 1.5-megadalton assemblage of 1–2 copies of each of 13 different subunits, as well as two diffusible activators. Despite extensive genetic and biochemical work on the APC, in-depth mechanistic studies of this complex have proved technically difficult. Three papers (two in this issue1,2, and one in Nature Structural & Molecular Biology3) provide insight into how the APC mediates ubiquitination of its substrates. The researchers report high-resolution structures of the APC that they obtained by electron microscopy (EM), generated from structures with different combinations of subunits, allowing them to infer the exact placement of many of its subunits.

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Figure 1: Structure of the yeast APC1,2,3.

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Authors and Affiliations

  1. Ian Foe and David Toczyski are in the Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94158-9001, USA.,

    Ian Foe & David Toczyski

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  1. Ian Foe
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  2. David Toczyski
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Correspondence to Ian Foe or David Toczyski.

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Foe, I., Toczyski, D. A new look for the APC. Nature 470, 182–183 (2011). https://doi.org/10.1038/470182a

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