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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 3. — Mapping the Pin1 interaction domain in SMRT. (A) Yeast two-hybrid mapping of the Pin1 interaction domain. Left, diagram of Gal4-DBD-SMRT fragments used; right, normalized β-galactosidase activity. Amino acids are indicated by numbers. Error bars represent ±SD. (B) GST pull down mapping of Pin1-interacting regions in SMRT. HeLa WCEs expressing the indicated HA-SMRT constructs were subjected to pull downs using GST–Pin1 and immunoblotted with anti-HA antibodies. (C) Schematic diagram of SMRT showing in vivo phosphorylation sites as mapped by mass spectrometry (*), Cdk consensus motifs (▾), and deletion constructs used in Fig. 3 D. Amino acids are indicated by numbers. (D) GST pull downs of N-terminal deletions of HA-SMRT. HeLa WCEs expressing the indicated HA-SMRT constructs were subjected to pull downs using GST–Pin1 and immunoblotted with anti-HA antibodies. (E) Phosphorylated SMRT interacts with Pin1 in vitro. HeLa WCEs expressing HA-SMRT (1,178–1,823) were subjected to pull downs using GST–Pin1 and immunoblotting with the indicated antibodies. WB, Western blot.