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. 2013 Dec 1;27(23):2531–2536. doi: 10.1101/gad.229195.113

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© 2013 Welcker et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.

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Figure 1. — Degrons cooperate to bind Fbw7 dimers. (A) Model of cyclin E bound to dimeric Fbw7 through both degrons. (B) 293A cells were cotransfected with Flag-Fbw7 and MYC-cyclin E as indicated, and lysates were immunoprecipitated with Flag antibody and blotted with tag antibodies. (*) Heavy chain. The vertical line indicates cropped lanes. (C) Cyclin E turnover by dimers (Fbw7α) or monomers (Fbw7α-ΔD). 293A cells were cotransfected as indicated and analyzed by Western blotting (PCNA-loading control). (D,E) A weakened T380 degron requires both the T62 degron and Fbw7 dimers for cyclin E turnover (D) and binding to Fbw7 (E). The assays are as in B and C. (F) Cyclin E's degrons cooperate in a ubiquitylation assay. Lysates expressing the indicated MYC-tagged cyclin E constructs were subjected to in vitro ubiquitylation and immunoblotted for cyclin E (MYC tag).