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. 2005 Mar 7;201(5):793–804. doi: 10.1084/jem.20042034

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Copyright © 2005, The Rockefeller University Press

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Figure 4. — PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. (A) The C- (aa 490–915) and N- (aa 1–490) terminal domains of HDAC7 were produced as GST fusion proteins (GST-HDAC7Cter and GST-HDAC7Nter, respectively) and immobilized on glutathione beads. Equal amounts of purified recombinant proteins were used in IVK assays with constitutively active recombinant PKD1. IVK reactions were analyzed by SDS-PAGE and Coomassie staining (left) before autoradiography (right). (B) Sequences around the four identified serines in HDAC7 match with the canonical PKD recognition motif. (C) GST fusion proteins corresponding to the sequences surrounding the four putative PKD phosphorylation sites in HDAC7 were used as substrates in independent IVK assays with constitutively active recombinant PKD1. Mutant fusion proteins harboring a serine to alanine substitution were used as controls. Reactions were resolved by SDS-PAGE and gel was stained with Coomassie, dried, and analyzed by autoradiography. The arrow indicates the radioactive band corresponding to autophosphorylated PKD1 (rPKD1).