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. 2011 May 30;10:68. doi: 10.1186/1476-4598-10-68

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Copyright ©2011 Rajendran et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Role of 14-3-3 phosphorylation status in HDAC3 binding. (A) Domains in 14-3-3 showing phosphorylation sites probed by immunoblotting. (B) Nuclear and cytoplasmic extracts from HCT116 cells treated with 15 μM SFN or DMSO were immunoblotted with phosphospecific antibodies to p-14-3-3(T323) and p-14-3-3(S58). (C) HDAC3 pull-downs, performed as in Figure 7, were followed by immunoblotting for p-14-3-3(T323), p-14-3-3(S58), and HDAC3. (D) Model for 14-3-3 interacting with HDAC3: repressive actions on the nuclear localization signal (NLS) in 14-3-3, plus possible activation of the nuclear export signal (NES), are proposed based on prior studies with class IIa HDACs [56].