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. 2008 Oct 6;183(1):49–61. doi: 10.1083/jcb.200806172

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© 2008 Stanya et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 4. — Mutations of Cdk sites in SMRT disrupt Pin1 interaction. (A) Phosphospecific antibodies recognize WT but not mutant SMRT. HeLa cells were transfected with either WT HA-SMRT (1,178–1,823) or a 3× mutant (S1241A/T1445A/S1469A), and WCEs were prepared for immunoblotting with the indicated antibodies. (B) Mutation of Cdk sites in SMRT disrupts Pin1 interaction in vitro. HeLa cells were transfected with HA-SMRT WT (1,012–2,507) or the 3× mutant, and WCEs were subjected to pull downs with GST–Pin1 and immunoblotted with α-HA antibodies. (C) Mutation of Cdk sites stabilizes SMRT. HeLa cells were transfected with HA-SMRT (1,178–1,823) or the 3× mutant and treated with 100 μg/ml CHX for the indicated times. WCEs were immunoblotted with the indicated antibodies. Left, immunoblot; right, quantification of SMRT levels normalized to actin levels.