In this paper 1, Figure 1 and the legend have been corrected to read as follows:
Figure 1
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CDKL5 interacts with, and phosphorylates, SMAD3 protein.A. Schematic representation of SMAD3 and mutant SMAD3 domains. The locations of MH1 domain (light gray), linker region, and MH2 domain (dark gray) are shown. B. Interaction between CDKL5 and SMAD3. HEK293T cells were co‐transfected with HA‐CDKL5 and wild‐type SMAD3‐FLAG or the indicated SMAD3 mutant‐FLAG plasmids, and cell lysates (Input) were immunoprecipitated with anti‐FLAG antibodies (IP). GAPDH was used as an internal control for Input. Immunoprecipitated proteins were detected by anti‐HA (CDKL5) and anti‐FLAG antibodies (SMAD3 and SMAD3 mutants). Arrows indicate co‐immunoprecipitated CDKL5. Lysates of cells overexpressing only HA‐CDKL5 (Input; lane 1) were immunoprecipitated with anti‐FLAG antibodies as a control (IP; lane 2). Irrelevant lanes were spliced out with a white space. C. SH‐SY5Y cells, infected with CDKL5‐FLAG adenoviral particles or GFP adenoviral particles as control, were lysed (Input) and immunoprecipitated with anti‐FLAG antibodies (IP). Immunoprecipitated CDKL5, SMAD3 and GFP were detected by anti‐CDKL5, anti‐SMAD3 and anti‐GFP antibodies, respectively. D. CDKL5 phosphorylates SMAD3 at the MH1 domain. Kinase assays were conducted with purified CDKL5DC (1‐498aa) and SMAD3 or SMAD3 mutants. Samples were resolved by SDS‐PAGE, transferred onto nitrocellulose membrane and exposed to film by autoradiography. CDKL5DC was detected with PonceauS staining (lower panel). E. Immunoprecipitated FLAG‐tagged wild‐type CDKL5 was subjected to an in vitro kinase assay to test its ability to phosphorylate purified SMAD3 and SMAD2. Samples were resolved by SDS‐PAGE, transferred onto nitrocellulose membrane and exposed to film by autoradiography. The same membrane was subjected to immunoblot analyses using anti‐ SMAD3 and SMAD2 antibodies.
Neither of these changes affects the data, results or conclusions of the article.
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