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. Author manuscript; available in PMC: 2012 Jan 30.
Published in final edited form as: Mol Cell Endocrinol. 2010 Oct 19;332(1-2):180–188. doi: 10.1016/j.mce.2010.10.010

Figure 5. A cluster of Erk2 phosphorylation sites regulate SMRTα self-association.

Figure 5

A. A schematic of the SMRTα (1788-1974) domain is presented; 7 Erk consensus phosphorylation sites (S/T-P) are highlighted. Mutant constructs bearing alanine substitutions at these positions (“X”) are indicated. The ability of the wild-type or mutant GST-SMRTα (1788-1974) construct to be shifted in mobility by incubation with Erk2 (middle panel) and to bind full-length 35S-SMRTα in a GST-pulldown (bottom panel) were determined as in Figure 4. B. The analysis of Erk2 phosphylation sites was extended to the larger SMRTα (1559-2050) domain, using the same methodology as in panel A.