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. 2017 Jun 20;7:3865. doi: 10.1038/s41598-017-04218-2

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Switch analysis performed using the minimal model. (A) Reaction network for the crucial switching part (following the labeling conventions Fig. 2). (B) The concentration plot for core species over time showing the switch occurring after proper spindle attachment (dashed line, cf. Fig. 3). (C) One-parameter bifurcation diagrams showing the activity of the MCC against the number of attached kinetochores using different rates k _M1 (labeled next to the curves). With a properly chosen rate, the dashed red lines clearly show that all kinetochores have to be attached to completely silence the MCC. To reengage the SAC, kinetochores have to reattach. If the rate drops below the estimated threshold, the SAC is silenced before all kinetochores are attached. (D) Securin concentration under different treatments for in-vitro (thick lines) and in-silico (thin lines). The green curve shows the wild-type, blue shows the influence of Mad2 targeting siRNA and red shows the influence of nocodazole. In all situations, securin degrades steadily, validating the rheostat switch hypothesis.